| Tag | Content |
|---|
| CPLM ID | CPLM-002197 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | L-threonine dehydratase biosynthetic IlvA |
Protein Synonyms/Alias | Threonine deaminase |
Gene Name | ilvA |
Gene Synonyms/Alias | b3772; JW3745 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 36 | AQVTPLQKMEKLSSR | acetylation | [1] | | 62 | RQPVHSFKLRGAYAM | acetylation | [1] | | 139 | GANFDEAKAKAIELS | acetylation | [1] | | 349 | AVTIPEEKGSFLKFC | acetylation | [1] | | 354 | EEKGSFLKFCQLLGG | acetylation | [1] | | 375 | NYRFADAKNACIFVG | 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 | Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short- lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. |
Sequence Annotation | DOMAIN 339 411 ACT-like 1.
DOMAIN 434 504 ACT-like 2.
REGION 189 192 Pyridoxal phosphate binding.
BINDING 89 89 Pyridoxal phosphate.
BINDING 315 315 Pyridoxal phosphate.
MOD_RES 62 62 N6-(pyridoxal phosphate)lysine. |
Keyword | 3D-structure; Allosteric enzyme; Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Complete proteome; Isoleucine biosynthesis; Lyase; Pyridoxal phosphate; Reference proteome; Repeat. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 514 AA |
Protein Sequence | MADSQPLSGA PEGAEYLRAV LRAPVYEAAQ VTPLQKMEKL SSRLDNVILV KREDRQPVHS 60
FKLRGAYAMM AGLTEEQKAH GVITASAGNH AQGVAFSSAR LGVKALIVMP TATADIKVDA 120
VRGFGGEVLL HGANFDEAKA KAIELSQQQG FTWVPPFDHP MVIAGQGTLA LELLQQDAHL 180
DRVFVPVGGG GLAAGVAVLI KQLMPQIKVI AVEAEDSACL KAALDAGHPV DLPRVGLFAE 240
GVAVKRIGDE TFRLCQEYLD DIITVDSDAI CAAMKDLFED VRAVAEPSGA LALAGMKKYI 300
ALHNIRGERL AHILSGANVN FHGLRYVSER CELGEQREAL LAVTIPEEKG SFLKFCQLLG 360
GRSVTEFNYR FADAKNACIF VGVRLSRGLE ERKEILQMLN DGGYSVVDLS DDEMAKLHVR 420
YMVGGRPSHP LQERLYSFEF PESPGALLRF LNTLGTYWNI SLFHYRSHGT DYGRVLAAFE 480
LGDHEPDFET RLNELGYDCH DETNNPAFRF FLAG 514 |
Gene Ontology | GO:0016597; F:amino acid binding; IDA:EcoliWiki. GO:0004794; F:L-threonine ammonia-lyase activity; IDA:EcoCyc. GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. GO:0009097; P:isoleucine biosynthetic process; IDA:EcoCyc. GO:0006566; P:threonine metabolic process; IDA:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |