Tag | Content |
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CPLM ID | CPLM-010191 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Low specificity L-threonine aldolase |
Protein Synonyms/Alias | Low specificity L-TA |
Gene Name | ltaE |
Gene Synonyms/Alias | ybjU; b0870; JW0854 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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119 | PLDKVAMKIKPDDIH | acetylation | [1] | 142 | LENTHNGKVLPREYL | acetylation | [1] | 150 | VLPREYLKEAWEFTR | acetylation | [1] | 215 | VGNRDYIKRAIRWRK | acetylation | [1] | 243 | AAGIYALKNNVARLQ | acetylation | [1] | 295 | AALGEYMKARNVLIN | acetylation | [1] |
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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 | Catalyzes the cleavage of L-allo-threonine and L- threonine to glycine and acetaldehyde. L-threo-phenylserine and L- erythro-phenylserine are also good substrates. |
Sequence Annotation | MOD_RES 197 197 N6-(pyridoxal phosphate)lysine (By |
Keyword | Complete proteome; Direct protein sequencing; Lyase; Pyridoxal phosphate; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 333 AA |
Protein Sequence | MIDLRSDTVT RPSRAMLEAM MAAPVGDDVY GDDPTVNALQ DYAAELSGKE AAIFLPTGTQ 60 ANLVALLSHC ERGEEYIVGQ AAHNYLFEAG GAAVLGSIQP QPIDAAADGT LPLDKVAMKI 120 KPDDIHFART KLLSLENTHN GKVLPREYLK EAWEFTRERN LALHVDGARI FNAVVAYGCE 180 LKEITQYCDS FTICLSKGLG TPVGSLLVGN RDYIKRAIRW RKMTGGGMRQ SGILAAAGIY 240 ALKNNVARLQ EDHDNAAWMA EQLREAGADV MRQDTNMLFV RVGEENAAAL GEYMKARNVL 300 INASPIVRLV THLDVSREQL AEVAAHWRAF LAR 333 |
Gene Ontology | GO:0008732; F:L-allo-threonine aldolase activity; IDA:EcoCyc. GO:0050179; F:phenylserine aldolase activity; IDA:EcoCyc. GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc. GO:0006545; P:glycine biosynthetic process; IGI:EcoCyc. |
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