CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
275RPFKHQEKDYLLYKFacetylation[1]
317DTLRLLEKIAPSAHKacetylation[1]
324KIAPSAHKIGASSAIacetylation[1]
363GSLIGLVKKHCEIWAacetylation[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
 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
 IPR011793; Carboxylate-amine_ligase_pred.
 IPR006336; GCS2. 
Pfam
 PF04107; GCS2 
SMART
  
PROSITE
  
PRINTS