Tag | Content |
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CPLM ID | CPLM-010299 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Carboxylate-amine ligase YbdK |
Protein Synonyms/Alias | |
Gene Name | ybdK |
Gene Synonyms/Alias | b0581; JW0570 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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275 | RPFKHQEKDYLLYKF | acetylation | [1] | 317 | DTLRLLEKIAPSAHK | acetylation | [1] | 324 | KIAPSAHKIGASSAI | acetylation | [1] | 363 | GSLIGLVKKHCEIWA | 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 | ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity. However, because of the low catalytic rate, the question remains whether L-cysteine is the actual biological substrate. |
Sequence Annotation | |
Keyword | 3D-structure; ATP-binding; Complete proteome; Ligase; Nucleotide-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 372 AA |
Protein Sequence | MPLPDFHVSE PFTLGIELEM QVVNPPGYDL SQDSSMLIDA VKNKITAGEV KHDITESMLE 60 LATDVCRDIN QAAGQFSAMQ KVVLQAATDH HLEICGGGTH PFQKWQRQEV CDNERYQRTL 120 ENFGYLIQQA TVFGQHVHVG CASGDDAIYL LHGLSRFVPH FIALSAASPY MQGTDTRFAS 180 SRPNIFSAFP DNGPMPWVSN WQQFEALFRC LSYTTMIDSI KDLHWDIRPS PHFGTVEVRV 240 MDTPLTLSHA VNMAGLIQAT AHWLLTERPF KHQEKDYLLY KFNRFQACRY GLEGVITDPH 300 TGDRRPLTED TLRLLEKIAP SAHKIGASSA IEALHRQVVS GLNEAQLMRD FVADGGSLIG 360 LVKKHCEIWA GD 372 |
Gene Ontology | GO:0005524; F:ATP binding; IDA:EcoCyc. GO:0004357; F:glutamate-cysteine ligase activity; IEA:InterPro. GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IDA:EcoCyc. GO:0042398; P:cellular modified amino acid biosynthetic process; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |