Adenylosuccinate lyase (P0AB89)

Identification
Name:Adenylosuccinate lyase
Synonyms:
  • ASL
  • Adenylosuccinase
  • ASase
Gene Name:purB
Enzyme Class:
Biological Properties
General Function:Involved in N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
Specific Function:N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP
Cellular Location:Not Available
SMPDB Pathways:
  • Aspartate metabolism PW000787
  • purine nucleotides de novo biosynthesis PW000910
  • purine nucleotides de novo biosynthesis 1435709748 PW000960
  • purine nucleotides de novo biosynthesis 2 PW002033
KEGG Pathways:
KEGG Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenylsuccinic acid ↔ 1.0Adenosine monophosphate + 1.0Fumaric acid
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1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0SAICAR ↔ 1.0Fumaric acid + 1.0AICAR
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1.0Thumb → 1.0Thumb+1.0Thumb
1.0SAICAR → 1.0Fumaric acid + 1.0AICAR
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenylsuccinic acid + 1.0SAICAR ↔ 1.0Fumaric acid + 1.0Adenosine monophosphate + 1.0AICAR
ReactionCard
SMPDB Reactions:
1.0N(6)-(1,2-dicarboxyethyl)AMP → 1.0Thumb+1.0Thumb
1.0N(6)-(1,2-dicarboxyethyl)AMP → 1.0Fumaric acid + 1.0Adenosine monophosphate
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1.0SAICAR+1.0Thumb → 1.0Thumb+1.0Thumb
1.0SAICAR + 1.0SAICAR → 1.0AICAR + 1.0Fumaric acid
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1.0N(6)-(1,2-dicarboxyethyl)AMP+1.0Thumb → 1.0Thumb+1.0Thumb
1.0N(6)-(1,2-dicarboxyethyl)AMP + 1.0Adenylsuccinic acid → 1.0Fumaric acid + 1.0Adenosine monophosphate
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EcoCyc Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.0SAICAR → 1.0Fumaric acid + 1.0AICAR
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Complex Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0SAICAR ↔ 1.0Phosphoribosyl formamidocarboxamide + 1.0Fumaric acid
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1.0Thumb → 1.0Thumb+1.0Thumb
1.0Adenylsuccinic acid → 1.0Fumaric acid + 1.0Adenosine monophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB01332Adenylsuccinic acidMetaboCard
ECMDB01517AICARMetaboCard
ECMDB00176Fumaric acidMetaboCard
ECMDB01439Phosphoribosyl formamidocarboxamideMetaboCard
ECMDB00797SAICARMetaboCard
GO Classification:
Function
amidine-lyase activity
carbon-nitrogen lyase activity
catalytic activity
lyase activity
N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
Process
cellular nitrogen compound metabolic process
IMP biosynthetic process
metabolic process
nitrogen compound metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
purine nucleoside monophosphate biosynthetic process
purine nucleotide biosynthetic process
purine nucleotide metabolic process
purine ribonucleoside monophosphate biosynthetic process
purine ribonucleotide biosynthetic process
Gene Properties
Blattner:b1131
Gene OrientationCounterclockwise
Centisome Percentage:25.64
Left Sequence End1189839
Right Sequence End1191209
Gene Sequence:
>1371 bp
ATGGAATTATCCTCACTGACCGCCGTTTCCCCTGTCGATGGACGCTACGGCGATAAAGTC
AGCGCGCTGCGCGGGATTTTCAGCGAATATGGTTTGCTGAAATTCCGTGTACAAGTTGAA
GTACGTTGGCTGCAAAAACTGGCCGCGCACGCAGCGATCAAGGAAGTTCCTGCTTTTGCT
GCCGACGCAATCGGTTACCTTGATGCAATCGTCGCCAGTTTCAGCGAAGAAGATGCGGCG
CGCATCAAAACTATCGAGCGTACCACTAACCACGACGTTAAAGCGGTTGAGTATTTCCTG
AAAGAAAAAGTGGCGGAGATCCCGGAACTGCACGCGGTTTCTGAATTCATCCACTTTGCC
TGTACTTCGGAAGATATCAATAACCTCTCCCACGCATTAATGCTGAAAACCGCGCGTGAT
GAAGTGATCCTGCCATACTGGCGTCAACTGATTGATGGCATTAAAGATCTCGCCGTTCAG
TATCGCGATATCCCGCTGCTGTCTCGTACCCACGGTCAGCCAGCCACGCCGTCAACCATC
GGTAAAGAGATGGCAAACGTCGCCTACCGTATGGAGCGCCAGTACCGCCAGCTTAACCAG
GTGGAGATCCTCGGCAAAATCAACGGCGCGGTCGGTAACTATAACGCCCACATCGCCGCT
TACCCGGAAGTTGACTGGCATCAGTTCAGCGAAGAGTTCGTCACCTCGCTGGGTATTCAG
TGGAACCCGTACACCACCCAGATCGAACCGCACGACTACATTGCCGAACTGTTTGATTGC
GTTGCGCGCTTCAACACTATTCTGATCGACTTTGACCGTGACGTCTGGGGTTATATCGCC
CTTAACCACTTCAAACAGAAAACCATTGCTGGTGAGATTGGTTCTTCCACCATGCCGCAT
AAAGTTAACCCGATCGACTTCGAAAACTCCGAAGGGAATCTGGGCCTTTCCAACGCGGTA
TTGCAGCATCTGGCAAGCAAACTGCCGGTTTCCCGCTGGCAGCGTGACCTGACCGACTCT
ACCGTGCTGCGTAACCTCGGCGTGGGTATCGGTTATGCCTTGATTGCATATCAATCCACC
CTGAAAGGCGTGAGCAAACTGGAAGTGAACCGTGACCATCTGCTGGATGAACTGGATCAC
AACTGGGAAGTGCTGGCTGAACCAATCCAGACAGTTATGCGTCGCTATGGCATCGAAAAA
CCGTACGAGAAGCTGAAAGAGCTGACTCGCGGTAAGCGCGTTGACGCCGAAGGCATGAAG
CAGTTTATCGATGGTCTGGCGTTGCCAGAAGAAGAGAAAGCCCGCCTGAAAGCGATGACG
CCGGCTAACTATATTGGTCGAGCTATCACGATGGTTGATGAGCTGAAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:456
Protein Molecular Weight:51542
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Adenylosuccinate lyase
MELSSLTAVSPVDGRYGDKVSALRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIKEVPAFA
ADAIGYLDAIVASFSEEDAARIKTIERTTNHDVKAVEYFLKEKVAEIPELHAVSEFIHFA
CTSEDINNLSHALMLKTARDEVILPYWRQLIDGIKDLAVQYRDIPLLSRTHGQPATPSTI
GKEMANVAYRMERQYRQLNQVEILGKINGAVGNYNAHIAAYPEVDWHQFSEEFVTSLGIQ
WNPYTTQIEPHDYIAELFDCVARFNTILIDFDRDVWGYIALNHFKQKTIAGEIGSSTMPH
KVNPIDFENSEGNLGLSNAVLQHLASKLPVSRWQRDLTDSTVLRNLGVGIGYALIAYQST
LKGVSKLEVNRDHLLDELDHNWEVLAEPIQTVMRRYGIEKPYEKLKELTRGKRVDAEGMK
QFIDGLALPEEEKARLKAMTPANYIGRAITMVDELK
References
External Links:
ResourceLink
Uniprot ID:P0AB89
Uniprot Name:PUR8_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651559
Ecogene ID:EG11314
Ecocyc:EG11314
ColiBase:b1131
Kegg Gene:b1131
EchoBASE ID:EB1290
CCDB:PUR8_ECOLI
BacMap:16129094
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • He, B., Smith, J. M., Zalkin, H. (1992). "Escherichia coli purB gene: cloning, nucleotide sequence, and regulation by purR." J Bacteriol 174:130-136. Pubmed: 1729205
  • Kasahara, M., Nakata, A., Shinagawa, H. (1992). "Molecular analysis of the Escherichia coli phoP-phoQ operon." J Bacteriol 174:492-498. Pubmed: 1729240
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842