adenylosuccinate lyase, partial [halophilic archaeon J07HB67]
Protein Classification
adenylosuccinate lyase family protein( domain architecture ID 1002653)
adenylosuccinate lyase catalyzes the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR), and the conversion of adenylosuccinate into adenosine monophosphate (AMP)
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| PRK09285 super family | cl35805 | adenylosuccinate lyase; Provisional |
2-264 | 7.71e-161 | |||||
adenylosuccinate lyase; Provisional The actual alignment was detected with superfamily member PRK09285: Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 454.21 E-value: 7.71e-161
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| Name | Accession | Description | Interval | E-value | |||||
| PRK09285 | PRK09285 | adenylosuccinate lyase; Provisional |
2-264 | 7.71e-161 | |||||
adenylosuccinate lyase; Provisional Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 454.21 E-value: 7.71e-161
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| PurB | cd01598 | PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
2-264 | 3.99e-139 | |||||
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the product of the purB gene in Escherichia coli, and related proteins. It is a member of the Lyase class I family of the Lyase_I superfamily. Members of the Lyase class I family function as homotetramers to catalyze similar beta-elimination reactions in which a Calpha-N or Calpha-O bond is cleaved with the subsequent release of fumarate as one of the products. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two non-sequential steps in the de novo purine biosynthesis pathway: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylosuccinate (SAMP) into adenosine monophosphate (AMP). Pssm-ID: 176470 [Multi-domain] Cd Length: 425 Bit Score: 397.76 E-value: 3.99e-139
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| PurB | COG0015 | Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
2-264 | 2.90e-98 | |||||
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part of the Pathway/BioSystem: Purine biosynthesis Pssm-ID: 439786 [Multi-domain] Cd Length: 436 Bit Score: 294.30 E-value: 2.90e-98
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| purB | TIGR00928 | adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
2-264 | 2.91e-66 | |||||
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that catalyzes step 8 in the purine biosynthesis pathway for de novo synthesis of IMP and also the final reaction in the two-step sequence from IMP to AMP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis] Pssm-ID: 273345 [Multi-domain] Cd Length: 435 Bit Score: 212.21 E-value: 2.91e-66
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| ASL_C | pfam08328 | Adenylosuccinate lyase C-terminal; This domain is found at the C-terminus of adenylosuccinate ... |
192-264 | 2.64e-39 | |||||
Adenylosuccinate lyase C-terminal; This domain is found at the C-terminus of adenylosuccinate lyase(ASL; PurB in E. coli). It has been identified in bacteria, eukaryotes and archaea and is found together with the lyase domain pfam00206. ASL catalyzes the cleavage of succinylaminoimidazole carboxamide ribotide to aminoimidazole carboxamide ribotide and fumarate and the cleavage of adenylosuccinate to adenylate and fumarate. Pssm-ID: 462430 [Multi-domain] Cd Length: 115 Bit Score: 132.56 E-value: 2.64e-39
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| Name | Accession | Description | Interval | E-value | |||||
| PRK09285 | PRK09285 | adenylosuccinate lyase; Provisional |
2-264 | 7.71e-161 | |||||
adenylosuccinate lyase; Provisional Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 454.21 E-value: 7.71e-161
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| PurB | cd01598 | PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
2-264 | 3.99e-139 | |||||
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the product of the purB gene in Escherichia coli, and related proteins. It is a member of the Lyase class I family of the Lyase_I superfamily. Members of the Lyase class I family function as homotetramers to catalyze similar beta-elimination reactions in which a Calpha-N or Calpha-O bond is cleaved with the subsequent release of fumarate as one of the products. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two non-sequential steps in the de novo purine biosynthesis pathway: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylosuccinate (SAMP) into adenosine monophosphate (AMP). Pssm-ID: 176470 [Multi-domain] Cd Length: 425 Bit Score: 397.76 E-value: 3.99e-139
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| PLN02848 | PLN02848 | adenylosuccinate lyase |
2-264 | 2.36e-104 | |||||
adenylosuccinate lyase Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 310.52 E-value: 2.36e-104
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| PurB | COG0015 | Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
2-264 | 2.90e-98 | |||||
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part of the Pathway/BioSystem: Purine biosynthesis Pssm-ID: 439786 [Multi-domain] Cd Length: 436 Bit Score: 294.30 E-value: 2.90e-98
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| Adenylsuccinate_lyase_like | cd01595 | Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
2-264 | 3.60e-84 | |||||
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. These proteins are members of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). pCMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone, in the beta-ketoadipate pathway. ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting. Pssm-ID: 176467 [Multi-domain] Cd Length: 381 Bit Score: 256.28 E-value: 3.60e-84
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| purB | TIGR00928 | adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
2-264 | 2.91e-66 | |||||
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that catalyzes step 8 in the purine biosynthesis pathway for de novo synthesis of IMP and also the final reaction in the two-step sequence from IMP to AMP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis] Pssm-ID: 273345 [Multi-domain] Cd Length: 435 Bit Score: 212.21 E-value: 2.91e-66
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| Lyase_I | cd01334 | Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
2-231 | 1.87e-46 | |||||
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; The Lyase class I family contains class II fumarase, aspartase, adenylosuccinate lyase (ASL), argininosuccinate lyase (ASAL), prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. It belongs to the Lyase_I superfamily. Proteins of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Pssm-ID: 176461 [Multi-domain] Cd Length: 325 Bit Score: 157.66 E-value: 1.87e-46
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| ASL_C | pfam08328 | Adenylosuccinate lyase C-terminal; This domain is found at the C-terminus of adenylosuccinate ... |
192-264 | 2.64e-39 | |||||
Adenylosuccinate lyase C-terminal; This domain is found at the C-terminus of adenylosuccinate lyase(ASL; PurB in E. coli). It has been identified in bacteria, eukaryotes and archaea and is found together with the lyase domain pfam00206. ASL catalyzes the cleavage of succinylaminoimidazole carboxamide ribotide to aminoimidazole carboxamide ribotide and fumarate and the cleavage of adenylosuccinate to adenylate and fumarate. Pssm-ID: 462430 [Multi-domain] Cd Length: 115 Bit Score: 132.56 E-value: 2.64e-39
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| Lyase_1 | pfam00206 | Lyase; |
2-170 | 1.06e-34 | |||||
Lyase; Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 126.71 E-value: 1.06e-34
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| Adenylsuccinate_lyase_1 | cd01360 | Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
2-264 | 2.35e-32 | |||||
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). Pssm-ID: 176464 [Multi-domain] Cd Length: 387 Bit Score: 121.89 E-value: 2.35e-32
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| Lyase_I_like | cd01594 | Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
2-223 | 8.22e-25 | |||||
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase, which catalyze similar beta-elimination reactions; Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively. Pssm-ID: 176466 [Multi-domain] Cd Length: 231 Bit Score: 98.45 E-value: 8.22e-25
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| pCLME | cd01597 | prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
2-264 | 1.47e-21 | |||||
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains pCLME and related proteins, and belongs to the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. CMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone in the beta-ketoadipate pathway. This pathway is responsible for the catabolism of a variety of aromatic compounds into intermediates of the citric cycle in prokaryotic and eukaryotic micro-organisms. Pssm-ID: 176469 [Multi-domain] Cd Length: 437 Bit Score: 93.08 E-value: 1.47e-21
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| protocat_pcaB | TIGR02426 | 3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis, ... |
1-166 | 2.06e-13 | |||||
3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis,cis-muconate cycloisomerase, the enzyme the catalyzes the second step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other] Pssm-ID: 274128 [Multi-domain] Cd Length: 338 Bit Score: 69.00 E-value: 2.06e-13
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| Fumarase_classII | cd01362 | Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
2-165 | 7.36e-13 | |||||
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle. Pssm-ID: 176465 [Multi-domain] Cd Length: 455 Bit Score: 67.53 E-value: 7.36e-13
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| fumC | PRK00485 | fumarate hydratase; Reviewed |
2-165 | 2.54e-12 | |||||
fumarate hydratase; Reviewed Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 66.27 E-value: 2.54e-12
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| PRK09053 | PRK09053 | 3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
2-166 | 3.01e-12 | |||||
3-carboxy-cis,cis-muconate cycloisomerase; Provisional Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 65.81 E-value: 3.01e-12
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| FumC | COG0114 | Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
2-165 | 2.76e-11 | |||||
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is part of the Pathway/BioSystem: TCA cycle Pssm-ID: 439884 [Multi-domain] Cd Length: 461 Bit Score: 63.12 E-value: 2.76e-11
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| Aspartase_like | cd01596 | aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
2-165 | 5.16e-11 | |||||
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains aspartase (L-aspartate ammonia-lyase), fumarase class II enzymes, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle. Pssm-ID: 176468 [Multi-domain] Cd Length: 450 Bit Score: 62.06 E-value: 5.16e-11
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| PLN00134 | PLN00134 | fumarate hydratase; Provisional |
2-169 | 1.24e-10 | |||||
fumarate hydratase; Provisional Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 61.24 E-value: 1.24e-10
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| PRK12425 | PRK12425 | class II fumarate hydratase; |
2-169 | 1.49e-10 | |||||
class II fumarate hydratase; Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 60.71 E-value: 1.49e-10
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| Adenylsuccinate_lyase_2 | cd03302 | Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
2-205 | 1.60e-10 | |||||
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting. Pssm-ID: 176471 [Multi-domain] Cd Length: 436 Bit Score: 60.79 E-value: 1.60e-10
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| Argininosuccinate_lyase | cd01359 | Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
5-165 | 4.69e-10 | |||||
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASAL is a cytosolic enzyme which catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate during arginine biosynthesis. In ureotelic species ASAL also catalyzes a reaction involved in the production of urea. Included in this group are the major soluble avian eye lens proteins from duck, delta 1 and delta 2 crystallin. Of these two isoforms only delta 2 has retained ASAL activity. These crystallins may have evolved by, gene recruitment of ASAL followed by gene duplication. In humans, mutations in ASAL result in the autosomal recessive disorder argininosuccinic aciduria. Pssm-ID: 176463 [Multi-domain] Cd Length: 435 Bit Score: 59.48 E-value: 4.69e-10
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| Aspartase | cd01357 | Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
2-166 | 6.41e-08 | |||||
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), Bacillus aspartase and related proteins. It is a member of the Lyase class I family, which includes both aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid. Pssm-ID: 176462 [Multi-domain] Cd Length: 450 Bit Score: 52.91 E-value: 6.41e-08
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| PRK06705 | PRK06705 | argininosuccinate lyase; Provisional |
15-178 | 1.34e-06 | |||||
argininosuccinate lyase; Provisional Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 48.83 E-value: 1.34e-06
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| PRK13353 | PRK13353 | aspartate ammonia-lyase; Provisional |
2-166 | 5.16e-06 | |||||
aspartate ammonia-lyase; Provisional Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 47.29 E-value: 5.16e-06
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| aspA | PRK12273 | aspartate ammonia-lyase; Provisional |
2-64 | 6.10e-06 | |||||
aspartate ammonia-lyase; Provisional Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 47.04 E-value: 6.10e-06
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| PRK08937 | PRK08937 | adenylosuccinate lyase; Provisional |
152-264 | 4.55e-05 | |||||
adenylosuccinate lyase; Provisional Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 43.48 E-value: 4.55e-05
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| PRK00855 | PRK00855 | argininosuccinate lyase; Provisional |
5-165 | 4.57e-05 | |||||
argininosuccinate lyase; Provisional Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 44.37 E-value: 4.57e-05
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| PRK05975 | PRK05975 | 3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
6-169 | 1.26e-04 | |||||
3-carboxy-cis,cis-muconate cycloisomerase; Provisional Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 42.73 E-value: 1.26e-04
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| Blast search parameters | ||||
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