FUCM_SALAR
ID FUCM_SALAR Reviewed; 140 AA.
AC A9MSA4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=SARI_04684;
OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=41514;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000880; ABX24448.1; -; Genomic_DNA.
DR RefSeq; WP_000920850.1; NC_010067.1.
DR AlphaFoldDB; A9MSA4; -.
DR SMR; A9MSA4; -.
DR STRING; 41514.SARI_04684; -.
DR EnsemblBacteria; ABX24448; ABX24448; SARI_04684.
DR KEGG; ses:SARI_04684; -.
DR HOGENOM; CLU_120075_1_0_6; -.
DR OMA; MGHGDDI; -.
DR OrthoDB; 1750843at2; -.
DR UniPathway; UPA00956; -.
DR Proteomes; UP000002084; 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..140
FT /note="L-fucose mutarotase"
FT /id="PRO_1000187190"
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; 15256 MW; CEFCB55C401838D3 CRC64;
MLKTISPLIS PTLLKVLAEM GHGDEIIFSD AHFPAQSLGP QVIRADGLSV SDLLRAIIPL
FELDNYAPPL VMMAAVEGDT LDPAVEARYR DALSLEAPCP DIVRIDRYAF YERAQKAFAI
VITGECAKYG NILLKKGVTP
