ID   FUCM_SALPK              Reviewed;         140 AA.
AC   B5BF33;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 63.
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}; OrderedLocusNames=SSPA2648;
OS   Salmonella paratyphi A (strain AKU_12601).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=554290;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AKU_12601;
RX   PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA   Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA   Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA   Mungall K., Dougan G., Parkhill J.;
RT   "Pseudogene accumulation in the evolutionary histories of Salmonella
RT   enterica serovars Paratyphi A and Typhi.";
RL   BMC Genomics 10:36-36(2009).
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; FM200053; CAR60890.1; -; Genomic_DNA.
DR   RefSeq; WP_000920848.1; NC_011147.1.
DR   AlphaFoldDB; B5BF33; -.
DR   SMR; B5BF33; -.
DR   KEGG; sek:SSPA2648; -.
DR   HOGENOM; CLU_120075_1_0_6; -.
DR   OMA; MGHGDDI; -.
DR   UniPathway; UPA00956; -.
DR   Proteomes; UP000001869; 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_1000187200"
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