UniProt Accession

 YIHX_ECOLI; P0A8Y3; P32145; Q2M8I2 

Genbank Protein ID

 L19201; U00096; AP009048 

Genbank Nucleotide ID

 AAB03018.1; AAD13447.2; BAE77424.1 

Protein Name

 Alpha-D-glucose-1-phosphate phosphatase YihX 

Protein Synonyms/Alias

 Alpha-D-glucose-1-P phosphatase 

Gene Name

 yihX 

Gene Synonyms/Alias

 b3885; JW5566 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
35	RIPLASLKKSFHMGE	acetylation	[1]
187	TSILVKDKTTIPDYF	acetylation	[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 dephosphorylation of alpha-D-glucose-1- phosphate (Glu1P) and has no activity with the beta form. In addition, YihX has phosphatase activity against sugar-phosphate and pyridoxal phosphate (PLP) and low beta-phosphoglucomutase activity. 

Sequence Annotation

 REGION 6 8 Substrate binding.
 REGION 107 108 Substrate binding.
 ACT_SITE 6 6 Nucleophile.
 METAL 6 6 Magnesium (By similarity).
 METAL 166 166 Magnesium (By similarity).
 BINDING 141 141 Substrate.
 BINDING 166 166 Substrate.  

Keyword

 3D-structure; Complete proteome; Hydrolase; Magnesium; Manganese; Metal-binding; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 199 AA 

Protein Sequence

Gene Ontology

 GO:0008877; F:glucose-1-phosphatase activity; IDA:EcoliWiki.
 GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
 GO:0030145; F:manganese ion binding; IDA:UniProtKB. 

Interpro

 IPR023214; HAD-like_dom.
 IPR006402; HAD-SF_hydro_IA_v3.
 IPR005833; Haloacid_DH/epoxide_hydro.
 IPR023198; PGP_dom2. 

Pfam

 PF13419; HAD_2 

SMART

  

PROSITE

  

PRINTS

 PR00413; HADHALOGNASE.