CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010182
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Sugar phosphatase YbiV 
Protein Synonyms/Alias
  
Gene Name
 ybiV 
Gene Synonyms/Alias
 supH; b0822; JW0806 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
19GTFLNDAKTYNQPRFacetylation[1]
34MAQYQELKKRGIKFVacetylation[1]
77ALVYEHGKQLFHGELacetylation[1]
98IVIGELLKDKQLNFVacetylation[1]
137YHRLKPVKDYQEIDDacetylation[1]
224GNDAEMLKMARYSFAacetylation[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 hydrolysis of sugar phosphate to sugar and inorganic phosphate. Has a wide substrate specificity catalyzing the hydrolysis of fructose-1-phosphate (Fru1P) most efficiently, but it remains uncertain if this is the real substrate in vivo. Appears to have a low level of phosphotransferase activity using monophosphates as the phosphate donor. 
Sequence Annotation
 REGION 9 11 Substrate (By similarity).
 REGION 44 46 Substrate binding.
 ACT_SITE 9 9 Nucleophile.
 METAL 9 9 Magnesium.
 METAL 11 11 Magnesium.
 METAL 215 215 Magnesium.
 METAL 216 216 Magnesium.
 BINDING 192 192 Substrate.  
Keyword
 3D-structure; Complete proteome; Hydrolase; Magnesium; Metal-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 271 AA 
Protein Sequence
MSVKVIVTDM DGTFLNDAKT YNQPRFMAQY QELKKRGIKF VVASGNQYYQ LISFFPELKD 60
EISFVAENGA LVYEHGKQLF HGELTRHESR IVIGELLKDK QLNFVACGLQ SAYVSENAPE 120
AFVALMAKHY HRLKPVKDYQ EIDDVLFKFS LNLPDEQIPL VIDKLHVALD GIMKPVTSGF 180
GFIDLIIPGL HKANGISRLL KRWDLSPQNV VAIGDSGNDA EMLKMARYSF AMGNAAENIK 240
QIARYATDDN NHEGALNVIQ AVLDNTSPFN S 271 
Gene Ontology
 GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
 GO:0050308; F:sugar-phosphatase activity; IDA:EcoCyc. 
Interpro
 IPR023214; HAD-like_dom.
 IPR006379; HAD-SF_hydro_IIB.
 IPR000150; Hypothet_cof. 
Pfam
 PF08282; Hydrolase_3 
SMART
  
PROSITE
 PS01228; COF_1
 PS01229; COF_2 
PRINTS