FUCM_ACTP2
ID FUCM_ACTP2 Reviewed; 144 AA.
AC A3N2Y4;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=APL_1686;
OS Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=416269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L20;
RX PubMed=18065534; DOI=10.1128/jb.01845-07;
RA Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA Nash J.H.E.;
RT "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT (serotype 5b).";
RL J. Bacteriol. 190:1495-1496(2008).
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; CP000569; ABN74770.1; -; Genomic_DNA.
DR RefSeq; WP_005605693.1; NC_009053.1.
DR AlphaFoldDB; A3N2Y4; -.
DR SMR; A3N2Y4; -.
DR STRING; 416269.APL_1686; -.
DR EnsemblBacteria; ABN74770; ABN74770; APL_1686.
DR KEGG; apl:APL_1686; -.
DR eggNOG; COG4154; Bacteria.
DR HOGENOM; CLU_120075_1_0_6; -.
DR OMA; MGHGDDI; -.
DR UniPathway; UPA00956; -.
DR Proteomes; UP000001432; 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;
KW Reference proteome.
FT CHAIN 1..144
FT /note="L-fucose mutarotase"
FT /id="PRO_0000344536"
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 109
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01662"
FT BINDING 131..133
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01662"
SQ SEQUENCE 144 AA; 15614 MW; A77E78E81DE711A9 CRC64;
MLKGIHPAIS PELLKVLAEM GHGDELVLSD AHFPAHSIHS KVIRADGIGV ATLLEGISAL
FEFDQYVEAP LAMMQAVPGD TLDPSVEERY LAAIKKVNGS TPKVERVERF AFYDRAKTAY
AVVITGELAK YGNIIIKKGV TPVK
