UniProt Accession

 FUCM_ECOLI; P0AEN8; P11555; Q2MA30; Q46923 

Genbank Protein ID

 X15025; U29581; U00096; AP009048 

Genbank Nucleotide ID

 CAA33129.1; AAB40454.1; AAC75846.1; BAE76876.1 

Protein Name

 L-fucose mutarotase 

Protein Synonyms/Alias

 Fucose 1-epimerase; Type-2 mutarotase 

Gene Name

 fucU 

Gene Synonyms/Alias

 b2804; JW2775 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
128	VITGERAKYGNILLK	acetylation	[1]
135	KYGNILLKKGVTP**	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

 Involved in the anomeric conversion of L-fucose. It also exhibits a pyranase activity for D-ribose. 

Sequence Annotation

 REGION 129 131 Substrate binding (By similarity).
 ACT_SITE 22 22 Proton donor (By similarity).
 BINDING 30 30 Substrate (By similarity).
 BINDING 107 107 Substrate (By similarity).  

Keyword

 3D-structure; Carbohydrate metabolism; Complete proteome; Cytoplasm; Fucose metabolism; Isomerase; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 140 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; ISS:EcoCyc.
 GO:0042806; F:fucose binding; IDA:MGI.
 GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; IDA:EcoCyc.
 GO:0042354; P:L-fucose metabolic process; IEA:HAMAP. 

Interpro

 IPR023751; L-fucose_mutarotase.
 IPR023750; RbsD-like.
 IPR007721; RbsD_FucU. 

Pfam

 PF05025; RbsD_FucU 

SMART

  

PROSITE

  

PRINTS