UniProt Accession

 GMHB_ECOLI; P63228; P31546 

Genbank Protein ID

 D15061; U00096; AP009048; U70214 

Genbank Nucleotide ID

 BAA03661.1; AAC73311.1; BAA77877.1; AAB08628.1 

Protein Name

 D,D-heptose 1,7-bisphosphate phosphatase 

Protein Synonyms/Alias

 D-glycero-D-manno-heptose 1,7-bisphosphate phosphatase; HBP phosphatase 

Gene Name

 gmhB 

Gene Synonyms/Alias

 yaeD; b0200; JW0196 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
159	KVLVRTGKPITPEAE	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

 Converts the D-glycero-beta-D-manno-heptose 1,7- bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1- phosphate (HBP) by removing the phosphate group at the C-7 position. Also catalyzes the dephosphorylation of fructose-1,6- bisphosphate (Fru1,6bisP). 

Sequence Annotation

 REGION 11 13 Substrate binding.
 REGION 19 22 Substrate binding.
 REGION 53 56 Substrate binding.
 REGION 110 111 Substrate binding.
 ACT_SITE 11 11 Nucleophile.
 ACT_SITE 13 13 Proton donor.
 METAL 11 11 Magnesium.
 METAL 13 13 Magnesium; via carbonyl oxygen.
 METAL 92 92 Zinc.
 METAL 94 94 Zinc; via amide nitrogen.
 METAL 107 107 Zinc.
 METAL 109 109 Zinc.
 METAL 136 136 Magnesium.
 METAL 137 137 Magnesium.
 BINDING 137 137 Substrate.  

Keyword

 3D-structure; Carbohydrate metabolism; Complete proteome; Cytoplasm; Hydrolase; Lipopolysaccharide biosynthesis; Magnesium; Metal-binding; Reference proteome; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 191 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0034200; F:D,D-heptose 1,7-bisphosphate phosphatase activity; IDA:UniProtKB.
 GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IDA:UniProtKB.
 GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0009244; P:lipopolysaccharide core region biosynthetic process; IMP:EcoCyc. 

Interpro

 IPR023214; HAD-like_dom.
 IPR006549; HAD-SF_hydro_IIIA.
 IPR004446; Heptose_bisP_phosphatase.
 IPR006543; Histidinol-phos. 

Pfam

  

SMART

  

PROSITE

  

PRINTS