CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002921
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphopentomutase 
Protein Synonyms/Alias
 Phosphodeoxyribomutase 
Gene Name
 deoB 
Gene Synonyms/Alias
 drm; thyR; b4383; JW4346 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
220ARPFIGDKAGNFQRTacetylation[1, 2]
250LQKLVDEKHGQVVSVacetylation[1, 2]
259GQVVSVGKIADIYANacetylation[2]
271YANCGITKKVKATGLacetylation[2]
274CGITKKVKATGLDALacetylation[1, 2]
287ALFDATIKEMKEAGDacetylation[1, 2, 3]
372PVLVYGPKVKPGSLGacetylation[2]
393DIGQTLAKYFGTSDMacetylation[2]
Reference
 [1] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111]
 [2] 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]
 [3] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842
Functional Description
 Phosphotransfer between the C1 and C5 carbon atoms of pentose. 
Sequence Annotation
 METAL 10 10 Manganese (By similarity).
 METAL 311 311 Manganese (By similarity).
 METAL 347 347 Manganese (By similarity).
 METAL 348 348 Manganese (By similarity).
 METAL 359 359 Manganese (By similarity).
 MOD_RES 287 287 N6-acetyllysine.  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Isomerase; Manganese; Metal-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 407 AA 
Protein Sequence
MKRAFIMVLD SFGIGATEDA ERFGDVGADT LGHIAEACAK GEADNGRKGP LNLPNLTRLG 60
LAKAHEGSTG FIPAGMDGNA EVIGAYAWAH EMSSGKDTPS GHWEIAGVPV LFEWGYFSDH 120
ENSFPQELLD KLVERANLPG YLGNCHSSGT VILDQLGEEH MKTGKPIFYT SADSVFQIAC 180
HEETFGLDKL YELCEIAREE LTNGGYNIGR VIARPFIGDK AGNFQRTGNR HDLAVEPPAP 240
TVLQKLVDEK HGQVVSVGKI ADIYANCGIT KKVKATGLDA LFDATIKEMK EAGDNTIVFT 300
NFVDFDSSWG HRRDVAGYAA GLELFDRRLP ELMSLLRDDD ILILTADHGC DPTWTGTDHT 360
REHIPVLVYG PKVKPGSLGH RETFADIGQT LAKYFGTSDM EYGKAMF 407 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0030145; F:manganese ion binding; IEA:HAMAP.
 GO:0008973; F:phosphopentomutase activity; IEA:HAMAP.
 GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0043094; P:cellular metabolic compound salvage; IEA:InterPro.
 GO:0009264; P:deoxyribonucleotide catabolic process; IEA:HAMAP.
 GO:0006974; P:response to DNA damage stimulus; IEP:EcoliWiki. 
Interpro
 IPR017849; Alkaline_Pase-like_a/b/a.
 IPR017850; Alkaline_phosphatase_core.
 IPR010045; DeoB.
 IPR006124; Metalloenzyme.
 IPR024052; Phosphopentomutase_DeoB_cap. 
Pfam
 PF01676; Metalloenzyme 
SMART
  
PROSITE
  
PRINTS