ID   FUCM_SALNS              Reviewed;         140 AA.
AC   B4T4X3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=L-fucose mutarotase {ECO:0000255|HAMAP-Rule:MF_01662};
DE            EC=5.1.3.29 {ECO:0000255|HAMAP-Rule:MF_01662};
DE   AltName: Full=Fucose 1-epimerase {ECO:0000255|HAMAP-Rule:MF_01662};
DE   AltName: Full=Type-2 mutarotase {ECO:0000255|HAMAP-Rule:MF_01662};
GN   Name=fucU {ECO:0000255|HAMAP-Rule:MF_01662};
GN   OrderedLocusNames=SNSL254_A3203;
OS   Salmonella newport (strain SL254).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=423368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL254;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- FUNCTION: Involved in the anomeric conversion of L-fucose.
CC       {ECO:0000255|HAMAP-Rule:MF_01662}.
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:0000255|HAMAP-Rule:MF_01662};
CC   -!- PATHWAY: Carbohydrate metabolism; L-fucose metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_01662}.
CC   -!- SUBUNIT: Homodecamer. {ECO:0000255|HAMAP-Rule:MF_01662}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01662}.
CC   -!- SIMILARITY: Belongs to the RbsD / FucU family. FucU mutarotase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01662}.
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DR   EMBL; CP001113; ACF62369.1; -; Genomic_DNA.
DR   RefSeq; WP_000920848.1; NZ_CCMR01000001.1.
DR   AlphaFoldDB; B4T4X3; -.
DR   SMR; B4T4X3; -.
DR   EnsemblBacteria; ACF62369; ACF62369; SNSL254_A3203.
DR   KEGG; see:SNSL254_A3203; -.
DR   HOGENOM; CLU_120075_1_0_6; -.
DR   OMA; MGHGDDI; -.
DR   UniPathway; UPA00956; -.
DR   Proteomes; UP000008824; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042806; F:fucose binding; IEA:InterPro.
DR   GO; GO:0036373; F:L-fucose mutarotase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042354; P:L-fucose metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1650.10; -; 1.
DR   HAMAP; MF_01662; L_fucose_rotase; 1.
DR   InterPro; IPR023751; L-fucose_mutarotase.
DR   InterPro; IPR023750; RbsD-like_sf.
DR   InterPro; IPR007721; RbsD_FucU.
DR   Pfam; PF05025; RbsD_FucU; 1.
DR   SUPFAM; SSF102546; SSF102546; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Fucose metabolism; Isomerase.
FT   CHAIN           1..140
FT                   /note="L-fucose mutarotase"
FT                   /id="PRO_1000187196"
FT   ACT_SITE        22
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01662"
FT   BINDING         30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01662"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01662"
FT   BINDING         129..131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01662"
SQ   SEQUENCE   140 AA;  15254 MW;  F80F469B5DC2F30D CRC64;
     MLKTISPLIS PTLLKVLAEM GHGDEIIFSD AHFPAHSLGP QVIRADGLSV SDLLRAIIPL
     FELDSYAPPL VMMAAVEGDT LDPSVEARYR DALSLEAPCP DIVRIDRYAF YERAQKAFAI
     VITGECAKYG NILLKKGVTP