FUCM_SALPA
ID FUCM_SALPA Reviewed; 140 AA.
AC Q5PEK7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=SPA2842;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV78690.1; -; Genomic_DNA.
DR RefSeq; WP_000920848.1; NC_006511.1.
DR AlphaFoldDB; Q5PEK7; -.
DR SMR; Q5PEK7; -.
DR EnsemblBacteria; AAV78690; AAV78690; SPA2842.
DR KEGG; spt:SPA2842; -.
DR HOGENOM; CLU_120075_1_0_6; -.
DR OMA; MGHGDDI; -.
DR UniPathway; UPA00956; -.
DR Proteomes; UP000008185; 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_1000187197"
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
