CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008458
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 L-Ala-D/L-Glu epimerase 
Protein Synonyms/Alias
 AE epimerase; AEE 
Gene Name
 ycjG 
Gene Synonyms/Alias
 ycjH; b1325; JW1318 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
5***MRTVKVFEEAWPacetylation[1]
80LTREELQKILPAGAAacetylation[1]
151GAKLLKVKLDNHLISacetylation[1]
247RYEMVNIKLDKTGGLacetylation[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 epimerization of L-Ala-D-Glu to L-Ala-L- Glu and has a role in the recycling of the murein peptide, of which L-Ala-D-Glu is a component. Is also able to catalyze the reverse reaction and the epimerization of all the L-Ala-X dipeptides, except L-Ala-L-Arg, L-Ala-L-Lys and L-Ala-L-Pro. Is also active with L-Gly-L-Glu, L-Phe-L-Glu, and L-Ser-L-Glu, but not with L-Glu-L-Glu, L-Lys-L-Glu, L-Pro-L-Glu, L-Lys-L-Ala, or D- Ala-D-Ala. 
Sequence Annotation
 ACT_SITE 151 151 Proton acceptor; specific for (R)-
 ACT_SITE 247 247 Proton acceptor; specific for (S)-
 METAL 176 176 Magnesium (By similarity).
 METAL 202 202 Magnesium (By similarity).
 METAL 225 225 Magnesium (By similarity).
 BINDING 124 124 Substrate (By similarity).
 BINDING 149 149 Substrate (By similarity).
 BINDING 275 275 Substrate; via carbonyl oxygen (By
 BINDING 297 297 Substrate (By similarity).
 BINDING 299 299 Substrate (By similarity).  
Keyword
 3D-structure; Cell wall biogenesis/degradation; Complete proteome; Isomerase; Magnesium; Metal-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 321 AA 
Protein Sequence
MRTVKVFEEA WPLHTPFVIA RGSRSEARVV VVELEEEGIK GTGECTPYPR YGESDASVMA 60
QIMSVVPQLE KGLTREELQK ILPAGAARNA LDCALWDLAA RRQQQSLADL IGITLPETVI 120
TAQTVVIGTP DQMANSASTL WQAGAKLLKV KLDNHLISER MVAIRTAVPD ATLIVDANES 180
WRAEGLAARC QLLADLGVAM LEQPLPAQDD AALENFIHPL PICADESCHT RSNLKALKGR 240
YEMVNIKLDK TGGLTEALAL ATEARAQGFS LMLGCMLCTS RAISAALPLV PQVSFADLDG 300
PTWLAVDVEP ALQFTTGELH L 321 
Gene Ontology
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0016855; F:racemase and epimerase activity, acting on amino acids and derivatives; IDA:EcoCyc.
 GO:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
 GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniPathway. 
Interpro
 IPR026911; AE_epimerase.
 IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
 IPR013342; Mandelate_racemase_C.
 IPR013341; Mandelate_racemase_N.
 IPR001354; MR_MLE. 
Pfam
 PF01188; MR_MLE
 PF02746; MR_MLE_N 
SMART
 SM00922; MR_MLE 
PROSITE
 PS00908; MR_MLE_1
 PS00909; MR_MLE_2 
PRINTS