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Conserved domains on  [gi|429564713|gb|AGA13634|]
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adenylosuccinate dehydrogenase, partial [Escherichia coli]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 2-158 2.88e-109

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member PRK01117:

Pssm-ID: 476819  Cd Length: 430  Bit Score: 317.37  E-value: 2.88e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713   2 AREKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNFQLVNYYKAEAVDYQKVLDDTMAVAD 81
Cdd:PRK01117 116 AREKARGKKKIGTTGRGIGPAYEDKVARRGIRVGDLLDPETFAEKLEENLEYKNFLLTKYYGAEAVDFEEILDEYLEYAE 195

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429564713  82 ILTSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTR 158
Cdd:PRK01117 196 RLKPYVTDTSLLLNDALKAGKRVLFEGAQGTLLDIDHGTYPFVTSSNTTAGGAATGSGVGPTKIDYVLGIAKAYTTR 272
 
Name Accession Description Interval E-value
PRK01117 PRK01117
adenylosuccinate synthetase; Provisional
 2-158 2.88e-109

adenylosuccinate synthetase; Provisional


Pssm-ID: 234904  Cd Length: 430  Bit Score: 317.37  E-value: 2.88e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713   2 AREKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNFQLVNYYKAEAVDYQKVLDDTMAVAD 81
Cdd:PRK01117 116 AREKARGKKKIGTTGRGIGPAYEDKVARRGIRVGDLLDPETFAEKLEENLEYKNFLLTKYYGAEAVDFEEILDEYLEYAE 195

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429564713  82 ILTSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTR 158
Cdd:PRK01117 196 RLKPYVTDTSLLLNDALKAGKRVLFEGAQGTLLDIDHGTYPFVTSSNTTAGGAATGSGVGPTKIDYVLGIAKAYTTR 272
PurA COG0104
Adenylosuccinate synthase [Nucleotide transport and metabolism]; Adenylosuccinate synthase is ...
 2-158 6.32e-103

Adenylosuccinate synthase [Nucleotide transport and metabolism]; Adenylosuccinate synthase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439874  Cd Length: 423  Bit Score: 301.16  E-value: 6.32e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713   2 AREKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNFQLVNYYKAEAVDYQKVLDDTMAVAD 81
Cdd:COG0104  114 AREEARGKKKIGTTGRGIGPAYEDKVARRGIRVGDLLDPEVLREKLEELLEYKNFLLEKLYGAEPLDFEELLEEYLEYAE 193

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429564713  82 ILTSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTR 158
Cdd:COG0104  194 RLKPYVADTSELLNEALKAGKKVLFEGAQGTLLDIDHGTYPYVTSSNTTAGGACTGSGVGPTKIDRVIGVVKAYTTR 270
Adenylsucc_synt pfam00709
Adenylosuccinate synthetase;
2-158 4.72e-94

Adenylosuccinate synthetase;


Pssm-ID: 459912  Cd Length: 417  Bit Score: 278.08  E-value: 4.72e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713    2 AREKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNFQLVNYYKaEAVDYQKVLDDTMAVAD 81
Cdd:pfam00709 112 LREEARGKKKIGTTGRGIGPAYSDKAARRGIRVGDLLDPEVFREKLEALLELKNKLLEKLYG-EPLDVEEELEELLEYAE 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429564713   82 ILTSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTR 158
Cdd:pfam00709 191 RLKPYVVDTSYFLNKALKEGKKILFEGAQGTLLDIDHGTYPYVTSSNTTAGGACTGLGIGPTKIDEVIGVVKAYTTR 267
Adenylsucc_synt smart00788
Adenylosuccinate synthetase; Adenylosuccinate synthetase plays an important role in purine ...
 4-158 2.14e-92

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: 273.97  E-value: 2.14e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713     4 EKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNFQLVNYYKAEAVDYQKVLDDTMAVADIL 83
Cdd:smart00788 112 DKAREKARIGTTGRGIGPAYEDKVARRGIRVGDLFDEEVLREKLEELLDYKNFLLKKLYGAEPVDVEEILEELLEYAERL 191

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 429564713    84 TSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTR 158
Cdd:smart00788 192 RPYVTDVSELLNEALKAGKKVLFEGAQGTLLDIDHGTYPYVTSSNTTAGGAATGAGIGPTRIDRVIGVVKAYTTR 266
purA TIGR00184
adenylosuccinate synthase; Alternate name IMP--aspartate ligase. [Purines, pyrimidines, ...
 1-158 4.62e-91

adenylosuccinate synthase; Alternate name IMP--aspartate ligase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 272949  Cd Length: 425  Bit Score: 270.96  E-value: 4.62e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713    1 NAREKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNFQLVNYYKAEAVDYQKVLDDTMAVA 80
Cdd:TIGR00184 111 KAREKSKLAKKIGTTGKGIGPAYEDKVARSGLRVGDLLDDEAFAEKAKNILEYLNEQLVKYYKDEGVDYEKKLDEYMKYA 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429564713   81 DILTSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTR 158
Cdd:TIGR00184 191 EELKPFVVDVSVELNEALDEGEKVLFEGAQGTMLDIDYGTYPYVTSSNTTAGGVATGVGIGPTKVDEVIGVFKAYTTR 268
AdSS cd03108
adenylosuccinate synthetase; Adenylosuccinate synthetase (AdSS) catalyzes the first step in ...
 2-158 3.18e-56

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: 178.46  E-value: 3.18e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713   2 AREKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDlfdketfaeklkevmeyhnfqlvnyykaeavdyqkvlddtmavad 81
Cdd:cd03108  115 LEEKERGGKKIGTTKRGIGPAYADKAARTGIRVGD--------------------------------------------- 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429564713  82 iltSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTR 158
Cdd:cd03108  150 ---PYVVDTVELLNEALKAGKKVLFEGAQGTLLDIDFGTYPYVTSSNTTAGGVCTGLGIPPRRVDRVIGVVKAYTTR 223
amino_Aden_PurZ NF038379
succino-amino-deoxyadenylate synthase PurZ;
4-146 3.45e-08

succino-amino-deoxyadenylate synthase PurZ;


Pssm-ID: 468496  Cd Length: 292  Bit Score: 51.22  E-value: 3.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713   4 EKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHnFQLVNYYKAeavdyqkvlddtmavadil 83
Cdd:NF038379 115 EEAGPMTKIGSTKKGIGAARAAKIRRNPSTLGDAEGDFGEGAVRDQPWEIA-ERVVDNALY------------------- 174

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429564713  84 tsmvvdvsdllDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVD 146
Cdd:NF038379 175 -----------DFALQAAERIQIEGTQGYSLGLHAGFYPYCTSRDCTPADFLADAGIPLPNVD 226
 
Name Accession Description Interval E-value
PRK01117 PRK01117
adenylosuccinate synthetase; Provisional
 2-158 2.88e-109

adenylosuccinate synthetase; Provisional


Pssm-ID: 234904  Cd Length: 430  Bit Score: 317.37  E-value: 2.88e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713   2 AREKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNFQLVNYYKAEAVDYQKVLDDTMAVAD 81
Cdd:PRK01117 116 AREKARGKKKIGTTGRGIGPAYEDKVARRGIRVGDLLDPETFAEKLEENLEYKNFLLTKYYGAEAVDFEEILDEYLEYAE 195

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429564713  82 ILTSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTR 158
Cdd:PRK01117 196 RLKPYVTDTSLLLNDALKAGKRVLFEGAQGTLLDIDHGTYPFVTSSNTTAGGAATGSGVGPTKIDYVLGIAKAYTTR 272
PurA COG0104
Adenylosuccinate synthase [Nucleotide transport and metabolism]; Adenylosuccinate synthase is ...
 2-158 6.32e-103

Adenylosuccinate synthase [Nucleotide transport and metabolism]; Adenylosuccinate synthase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439874  Cd Length: 423  Bit Score: 301.16  E-value: 6.32e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713   2 AREKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNFQLVNYYKAEAVDYQKVLDDTMAVAD 81
Cdd:COG0104  114 AREEARGKKKIGTTGRGIGPAYEDKVARRGIRVGDLLDPEVLREKLEELLEYKNFLLEKLYGAEPLDFEELLEEYLEYAE 193

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429564713  82 ILTSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTR 158
Cdd:COG0104  194 RLKPYVADTSELLNEALKAGKKVLFEGAQGTLLDIDHGTYPYVTSSNTTAGGACTGSGVGPTKIDRVIGVVKAYTTR 270
Adenylsucc_synt pfam00709
Adenylosuccinate synthetase;
2-158 4.72e-94

Adenylosuccinate synthetase;


Pssm-ID: 459912  Cd Length: 417  Bit Score: 278.08  E-value: 4.72e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713    2 AREKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNFQLVNYYKaEAVDYQKVLDDTMAVAD 81
Cdd:pfam00709 112 LREEARGKKKIGTTGRGIGPAYSDKAARRGIRVGDLLDPEVFREKLEALLELKNKLLEKLYG-EPLDVEEELEELLEYAE 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429564713   82 ILTSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTR 158
Cdd:pfam00709 191 RLKPYVVDTSYFLNKALKEGKKILFEGAQGTLLDIDHGTYPYVTSSNTTAGGACTGLGIGPTKIDEVIGVVKAYTTR 267
Adenylsucc_synt smart00788
Adenylosuccinate synthetase; Adenylosuccinate synthetase plays an important role in purine ...
 4-158 2.14e-92

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: 273.97  E-value: 2.14e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713     4 EKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNFQLVNYYKAEAVDYQKVLDDTMAVADIL 83
Cdd:smart00788 112 DKAREKARIGTTGRGIGPAYEDKVARRGIRVGDLFDEEVLREKLEELLDYKNFLLKKLYGAEPVDVEEILEELLEYAERL 191

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 429564713    84 TSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTR 158
Cdd:smart00788 192 RPYVTDVSELLNEALKAGKKVLFEGAQGTLLDIDHGTYPYVTSSNTTAGGAATGAGIGPTRIDRVIGVVKAYTTR 266
purA TIGR00184
adenylosuccinate synthase; Alternate name IMP--aspartate ligase. [Purines, pyrimidines, ...
 1-158 4.62e-91

adenylosuccinate synthase; Alternate name IMP--aspartate ligase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 272949  Cd Length: 425  Bit Score: 270.96  E-value: 4.62e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713    1 NAREKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNFQLVNYYKAEAVDYQKVLDDTMAVA 80
Cdd:TIGR00184 111 KAREKSKLAKKIGTTGKGIGPAYEDKVARSGLRVGDLLDDEAFAEKAKNILEYLNEQLVKYYKDEGVDYEKKLDEYMKYA 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429564713   81 DILTSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTR 158
Cdd:TIGR00184 191 EELKPFVVDVSVELNEALDEGEKVLFEGAQGTMLDIDYGTYPYVTSSNTTAGGVATGVGIGPTKVDEVIGVFKAYTTR 268
PLN02513 PLN02513
adenylosuccinate synthase
 2-158 7.73e-60

adenylosuccinate synthase


Pssm-ID: 178129  Cd Length: 427  Bit Score: 191.01  E-value: 7.73e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713   2 AREKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNFQLvNYYKAEAVDYQKVLDDTMAVAD 81
Cdd:PLN02513 118 LREAELAGSKIGTTKRGIGPAYSSKATRNGLRVGDLRHMDTFAEKLRELLADAAARF-EGFEYDASMVEEEVEAYKKFAE 196

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429564713  82 ILTSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTR 158
Cdd:PLN02513 197 RLEPFITDTVHYLNEAIQAGKKILVEGAQATMLDIDFGTYPFVTSSNPSAGGICTGLGIAPRKLGDIIGVVKAYTTR 273
AdSS cd03108
adenylosuccinate synthetase; Adenylosuccinate synthetase (AdSS) catalyzes the first step in ...
 2-158 3.18e-56

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: 178.46  E-value: 3.18e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713   2 AREKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDlfdketfaeklkevmeyhnfqlvnyykaeavdyqkvlddtmavad 81
Cdd:cd03108  115 LEEKERGGKKIGTTKRGIGPAYADKAARTGIRVGD--------------------------------------------- 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429564713  82 iltSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTR 158
Cdd:cd03108  150 ---PYVVDTVELLNEALKAGKKVLFEGAQGTLLDIDFGTYPYVTSSNTTAGGVCTGLGIPPRRVDRVIGVVKAYTTR 223
PTZ00350 PTZ00350
adenylosuccinate synthetase; Provisional
 4-158 3.97e-53

adenylosuccinate synthetase; Provisional


Pssm-ID: 240376  Cd Length: 436  Bit Score: 173.68  E-value: 3.97e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713   4 EKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNFQlvnyYKAEAVDYQKVLDDTMAVADIL 83
Cdd:PTZ00350 131 EKGKGGTQIGTTKRGIGPCYSTKASRTGLRVGDLLNFETFEKKYRKLVEKLQEQ----YNIEEYDAEEELERYKGYAEKL 206

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 429564713  84 TSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTR 158
Cdd:PTZ00350 207 KDMIVDTVYFMNKAIKEGKRVLVEGANATMLDIDFGTYPYVTSSNTTVGGVCTGLGIPPNAIILVIGVVKAYTTR 281
PRK13785 PRK13785
adenylosuccinate synthetase; Provisional
 5-158 8.26e-45

adenylosuccinate synthetase; Provisional


Pssm-ID: 237506  Cd Length: 454  Bit Score: 152.61  E-value: 8.26e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713   5 KARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNFQLVNYY------KAEAVDYQKVLDDTMA 78
Cdd:PRK13785 117 KSDSDLEVGTTGRGIGPTYEDKAGRRGVRVGDLLDPDVLRDRLEYVVPQKRALAEDVYgldaseTPEAFDVDALFEEYRE 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713  79 VADILTS--MVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDY--VLGILKA 154
Cdd:PRK13785 197 YGERLAEedMTVNAGDFLAERIDDGDNVMLEGAQGTSIDIDHGNYPYVTSSNPTAGGAATGTGLGPTVVGQgeVVGIVKA 276


                 ....
gi 429564713 155 YSTR 158
Cdd:PRK13785 277 YLSR 280
PRK13783 PRK13783
adenylosuccinate synthetase; Provisional
 4-158 2.57e-42

adenylosuccinate synthetase; Provisional


Pssm-ID: 237505  Cd Length: 404  Bit Score: 144.86  E-value: 2.57e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713   4 EKARGaKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNfqlvNYYKAEaVDYQKVLDDTMAVADIL 83
Cdd:PRK13783 117 ESVRK-NAIGTTKRGIGPAYADKVMRVGVRLADLFDEEKLREFLEKILSLYK----KLYGIE-FDVEKMMEDLLTFYEKI 190

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 429564713  84 TSMVVDVSDLLDQARQRGdfVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLgPRYVDYVLGILKAYSTR 158
Cdd:PRK13783 191 KDLVVSPVEIKRILEEKS--VLFEGTQGVLLDLDVGTYPYVTSSNCSTTGVSAGMGF-PVKVDEVIGVFKAYTTR 262
PRK13787 PRK13787
adenylosuccinate synthetase; Provisional
 12-158 3.71e-41

adenylosuccinate synthetase; Provisional


Pssm-ID: 172324  Cd Length: 423  Bit Score: 142.40  E-value: 3.71e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713  12 IGTTGRGIGPAYEDKVARRGLRVGDLFDKeTFAEKLKEVMEYHNFQLVNYYKAEAVDYQKVLDDTMAVADILTSMVVDVS 91
Cdd:PRK13787 127 IGTTKKGIGICYADKMMRTGLRVGDLLDK-SYKRRLKHLVDEKNRELDKLYGMPPVSYNDINDGLKFFLSKVGKNIINTA 205

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429564713  92 DLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTR 158
Cdd:PRK13787 206 YYLDTELKKGKRVLLEGAQGTGLDVDFGTYPYVTSSNPTTGGALIGTGISFQHLKHVIGITKAYTTR 272
PRK13788 PRK13788
adenylosuccinate synthetase; Provisional
 12-158 1.28e-36

adenylosuccinate synthetase; Provisional


Pssm-ID: 184326 [Multi-domain]  Cd Length: 404  Bit Score: 129.93  E-value: 1.28e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713  12 IGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEyhnfQLVNYYKAEAVD-YQKVLDDTMAVADILTSMVVDV 90
Cdd:PRK13788 118 VGTTGRGIGPAYSDRARRVGIRFGDLLDEAVLRERVERLLE----AKPNSTREAGWDtVEKALADLAPMREILLPFIADT 193

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429564713  91 SDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTR 158
Cdd:PRK13788 194 GSLLREAIREGKRVLFEGAQATLLDLNYGTYPYVTSSHPTVGGILVGAGVNHKAINKVYGVAKAFTTR 261
PRK13784 PRK13784
adenylosuccinate synthetase; Provisional
 1-158 3.53e-34

adenylosuccinate synthetase; Provisional


Pssm-ID: 172322  Cd Length: 428  Bit Score: 123.98  E-value: 3.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713   1 NAREKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNFQLVNYYKAEAVDYQKVLDDTMAVA 80
Cdd:PRK13784 115 DAVRESNTSEKIGTTGKGIGPAYEDKVSRKGIKFKHLFDKDLLRSRLAISLAEKETLFRDLYKVEYPTLEQEFDKLFALG 194

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429564713  81 DILTSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTR 158
Cdd:PRK13784 195 QKLKQYAADTFSIIDQAIAAGKNVVYEGAQGVLLDVDYGTYPFVTSSNTSVAGVYSGATTAGHGLDHVIGITKAYTTR 272
PRK13786 PRK13786
adenylosuccinate synthetase; Provisional
 1-158 1.68e-33

adenylosuccinate synthetase; Provisional


Pssm-ID: 184325  Cd Length: 424  Bit Score: 121.83  E-value: 1.68e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713   1 NAREKARGAKaIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEyhnfQLVNYYKAEAVDYQKVLDDTM--- 77
Cdd:PRK13786 114 GLRESARTEK-IGTTKRGIGFAYIDKIARDEVRMSDLVDKERLMRRLEELAP----QKEKEIKELGGDPSIVRDEALidk 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713  78 --AVADILTSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAY 155
Cdd:PRK13786 189 ylELGRQLAPYITDVSYEINKALDEGKSVLAEGAQGTHLDVIHGTQKFVTSSSTIAGSACANLGVGPTRVDNVLGIVKAY 268


                 ...
gi 429564713 156 STR 158
Cdd:PRK13786 269 ITR 271
PRK04293 PRK04293
adenylosuccinate synthetase; Provisional
 9-158 3.90e-27

adenylosuccinate synthetase; Provisional


Pssm-ID: 179812  Cd Length: 333  Bit Score: 103.42  E-value: 3.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713   9 AKAIGTTGRGIGPAYEDKVARRGlrvgdlfdketfaeKLkevmeyhnfqlvnyykaeAVDYqkvlddtmavaDILTSMVV 88
Cdd:PRK04293 118 SKKIGSTGTGCGPANADRVLRRL--------------KL------------------AKDV-----------EELEKYLT 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713  89 DVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTR 158
Cdd:PRK04293 155 DVPEEVNEALDRGENVLIEGTQGFGLSLYYGTYPYVTSKDTTASGIASDVGVGPTKVDEVIVVFKSYPTR 224
amino_Aden_PurZ NF038379
succino-amino-deoxyadenylate synthase PurZ;
4-146 3.45e-08

succino-amino-deoxyadenylate synthase PurZ;


Pssm-ID: 468496  Cd Length: 292  Bit Score: 51.22  E-value: 3.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429564713   4 EKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHnFQLVNYYKAeavdyqkvlddtmavadil 83
Cdd:NF038379 115 EEAGPMTKIGSTKKGIGAARAAKIRRNPSTLGDAEGDFGEGAVRDQPWEIA-ERVVDNALY------------------- 174

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429564713  84 tsmvvdvsdllDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVD 146
Cdd:NF038379 175 -----------DFALQAAERIQIEGTQGYSLGLHAGFYPYCTSRDCTPADFLADAGIPLPNVD 226
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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