| Tag | Content |
|---|
| CPLM ID | CPLM-003147 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | L-asparaginase 1 |
Protein Synonyms/Alias | L-asparaginase I; L-ASNase I; L-asparagine amidohydrolase I |
Gene Name | ansA |
Gene Synonyms/Alias | b1767; JW1756 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 251 | VGNAPQNKAFLQELQ | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | |
Sequence Annotation | REGION 59 61 Substrate binding.
REGION 91 92 Substrate binding.
REGION 271 273 Allosteric activator binding.
ACT_SITE 14 14 O-isoaspartyl threonine intermediate.
BINDING 162 162 Allosteric activator.
BINDING 240 240 Allosteric activator. |
Keyword | 3D-structure; Allosteric enzyme; Complete proteome; Cytoplasm; Hydrolase; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 338 AA |
Protein Sequence | MQKKSIYVAY TGGTIGMQRS EQGYIPVSGH LQRQLALMPE FHRPEMPDFT IHEYTPLMDS 60
SDMTPEDWQH IAEDIKAHYD DYDGFVILHG TDTMAYTASA LSFMLENLGK PVIVTGSQIP 120
LAELRSDGQI NLLNALYVAA NYPINEVTLF FNNRLYRGNR TTKAHADGFD AFASPNLPPL 180
LEAGIHIRRL NTPPAPHGEG ELIVHPITPQ PIGVVTIYPG ISADVVRNFL RQPVKALILR 240
SYGVGNAPQN KAFLQELQEA SDRGIVVVNL TQCMSGKVNM GGYATGNALA HAGVIGGADM 300
TVEATLTKLH YLLSQELDTE TIRKAMSQNL RGELTPDD 338 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:EcoCyc. GO:0004067; F:asparaginase activity; IDA:EcoCyc. GO:0042802; F:identical protein binding; IDA:EcoCyc. GO:0033345; P:asparagine catabolic process via L-aspartate; IMP:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |