UniProt Accession

 F16PA_ECOLI; P0A993; P09200; Q2M674 

Genbank Protein ID

 X12545; U14003; U00096; AP009048 

Genbank Nucleotide ID

 CAA31062.1; AAA97129.1; AAC77189.1; BAE78232.1 

Protein Name

 Fructose-1,6-bisphosphatase class 1 

Protein Synonyms/Alias

 FBPase class 1; D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1 

Gene Name

 fbp 

Gene Synonyms/Alias

 fdp; b4232; JW4191 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
11	LGEFIVEKQHEFSHA	acetylation	[1]
30	TALLSAIKLGAKIIH	acetylation	[1, 2]
34	SAIKLGAKIIHRDIN	acetylation	[1]
42	IIHRDINKAGLVDIL	acetylation	[1]
72	LDLFANEKLKAALKA	acetylation	[1]
212	INEGNYIKFPNGVKK	acetylation	[1]
219	KFPNGVKKYIKFCQE	acetylation	[1]
222	NGVKKYIKFCQEEDK	acetylation	[1]
229	KFCQEEDKSTNRPYT	acetylation	[1]
269	TASHPDGKLRLLYEC	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]
 [2] 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] 

Functional Description

  

Sequence Annotation

 NP_BIND 19 23 AMP.
 NP_BIND 104 105 AMP.
 REGION 3 5 Allosteric activator binding.
 REGION 113 116 Substrate binding.
 REGION 257 259 Substrate binding.
 METAL 89 89 Magnesium 1.
 METAL 110 110 Magnesium 1.
 METAL 110 110 Magnesium 2.
 METAL 112 112 Magnesium 1; via carbonyl oxygen.
 METAL 113 113 Magnesium 2.
 METAL 275 275 Magnesium 2.
 BINDING 30 30 Allosteric activator.
 BINDING 187 187 Allosteric activator; via amide nitrogen.
 BINDING 206 206 Substrate.
 BINDING 222 222 Allosteric inhibitor glucose-6-phosphate.
 BINDING 225 225 Allosteric inhibitor glucose-6-phosphate.
 BINDING 239 239 Substrate.
 BINDING 269 269 Substrate.  

Keyword

 3D-structure; Allosteric enzyme; Carbohydrate metabolism; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Magnesium; Metal-binding; Nucleotide-binding; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 332 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IDA:EcoCyc.
 GO:0000287; F:magnesium ion binding; IEA:HAMAP.
 GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
 GO:0006094; P:gluconeogenesis; IMP:EcoCyc.
 GO:0019253; P:reductive pentose-phosphate cycle; IEA:HAMAP. 

Interpro

 IPR000146; FBPase_class-1/SBPase.
 IPR020548; Fructose_bisphosphatase_AS. 

Pfam

 PF00316; FBPase 

SMART

  

PROSITE

 PS00124; FBPASE 

PRINTS

 PR00115; F16BPHPHTASE.