ID   FUCM_BOVIN              Reviewed;         153 AA.
AC   Q0P563;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Fucose mutarotase;
DE            EC=5.1.3.29 {ECO:0000250|UniProtKB:Q8R2K1};
GN   Name=FUOM;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the interconversion between alpha- and beta-L-
CC       fucoses. L-Fucose (6-deoxy-L-galactose) exists as alpha-L-fucose
CC       (29.5%) and beta-L-fucose (70.5%), the beta-form is metabolized through
CC       the salvage pathway. GDP-L-fucose formed either by the de novo or
CC       salvage pathways is transported into the endoplasmic reticulum, where
CC       it serves as a substrate for N- and O-glycosylations by
CC       fucosyltransferases. Fucosylated structures expressed on cell surfaces
CC       or secreted in biological fluids are believed to play a critical role
CC       in cell-cell adhesion and recognition processes.
CC       {ECO:0000250|UniProtKB:Q8R2K1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-L-fucose = beta-L-fucose; Xref=Rhea:RHEA:25580,
CC         ChEBI:CHEBI:42548, ChEBI:CHEBI:42589; EC=5.1.3.29;
CC         Evidence={ECO:0000250|UniProtKB:Q8R2K1};
CC   -!- PATHWAY: Carbohydrate metabolism; L-fucose metabolism.
CC       {ECO:0000250|UniProtKB:Q8R2K1}.
CC   -!- SUBUNIT: Mainly homodimer, but exists also as homotetramer,
CC       homooctamer, and homodecamer. The homodimeric form seems catalytically
CC       inactive. {ECO:0000250|UniProtKB:Q8R2K1}.
CC   -!- SIMILARITY: Belongs to the RbsD / FucU family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC120455; AAI20456.1; -; mRNA.
DR   RefSeq; NP_001069746.1; NM_001076278.1.
DR   AlphaFoldDB; Q0P563; -.
DR   SMR; Q0P563; -.
DR   STRING; 9913.ENSBTAP00000007505; -.
DR   PaxDb; Q0P563; -.
DR   PRIDE; Q0P563; -.
DR   GeneID; 613571; -.
DR   KEGG; bta:613571; -.
DR   CTD; 282969; -.
DR   eggNOG; ENOG502RZR7; Eukaryota.
DR   InParanoid; Q0P563; -.
DR   OrthoDB; 1457717at2759; -.
DR   UniPathway; UPA00956; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0042806; F:fucose binding; ISS:UniProtKB.
DR   GO; GO:0036373; F:L-fucose mutarotase activity; ISS:UniProtKB.
DR   GO; GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; ISS:UniProtKB.
DR   GO; GO:0006004; P:fucose metabolic process; ISS:UniProtKB.
DR   GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR   Gene3D; 3.40.1650.10; -; 1.
DR   InterPro; IPR023750; RbsD-like_sf.
DR   InterPro; IPR007721; RbsD_FucU.
DR   Pfam; PF05025; RbsD_FucU; 1.
DR   SUPFAM; SSF102546; SSF102546; 1.
PE   2: Evidence at transcript level;
KW   Isomerase; Reference proteome.
FT   CHAIN           1..153
FT                   /note="Fucose mutarotase"
FT                   /id="PRO_0000286552"
FT   ACT_SITE        24
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R2K1"
FT   ACT_SITE        69
FT                   /evidence="ECO:0000250|UniProtKB:Q8R2K1"
FT   ACT_SITE        119
FT                   /evidence="ECO:0000250|UniProtKB:Q8R2K1"
FT   BINDING         32
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R2K1"
FT   BINDING         79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R2K1"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R2K1"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R2K1"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R2K1"
SQ   SEQUENCE   153 AA;  16469 MW;  903D2E85EC3126DA CRC64;
     MVVLKGVPAL LSPELLFALA RMGHGDEIVL ADVNFPSSSI CRGGPEEIRA DGLGIPQLLE
     AVLQLLPLDT YVQSPAMVME LVPSDRKSGL LTPVWTSYQS ILSRAGYEFS LGMGRFAFYE
     RAKKAFAVVA TGETALYGNL ILKKGVLAPK DLC