| Tag | Content |
|---|
| CPLM ID | CPLM-010366 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Methionine aminotransferase |
Protein Synonyms/Alias | Methionine-oxo-acid transaminase |
Gene Name | ybdL |
Gene Synonyms/Alias | b0600; JW0593 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 236 | VAVSSFGKTYHMTGW | 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 | Shows aminotransferase activity with methionine and histidine as substrates, and to a lesser extent also with phenylalanine. |
Sequence Annotation | MOD_RES 236 236 N6-(pyridoxal phosphate)lysine. |
Keyword | 3D-structure; Aminotransferase; Complete proteome; Cytoplasm; Pyridoxal phosphate; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 386 AA |
Protein Sequence | MTNNPLIPQS KLPQLGTTIF TQMSALAQQH QAINLSQGFP DFDGPRYLQE RLAHHVAQGA 60
NQYAPMTGVQ ALREAIAQKT ERLYGYQPDA DSDITVTAGA TEALYAAITA LVRNGDEVIC 120
FDPSYDSYAP AIALSGGIVK RMALQPPHFR VDWQEFAALL SERTRLVILN TPHNPSATVW 180
QQADFAALWQ AIAGHEIFVI SDEVYEHINF SQQGHASVLA HPQLRERAVA VSSFGKTYHM 240
TGWKVGYCVA PAPISAEIRK VHQYLTFSVN TPAQLALADM LRAEPEHYLA LPDFYRQKRD 300
ILVNALNESR LEILPCEGTY FLLVDYSAVS TLDDVEFCQW LTQEHGVAAI PLSVFCADPF 360
PHKLIRLCFA KKESTLLAAA ERLRQL 386 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0010326; F:methionine-oxo-acid transaminase activity; IDA:EcoCyc. GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc. GO:0009058; P:biosynthetic process; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |