FUCM_HAEI8
ID FUCM_HAEI8 Reviewed; 144 AA.
AC Q4QMI4;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=NTHI0867;
OS Haemophilus influenzae (strain 86-028NP).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=281310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=86-028NP;
RX PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA Munson R.S. Jr.;
RT "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL J. Bacteriol. 187:4627-4636(2005).
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; CP000057; AAX87763.1; -; Genomic_DNA.
DR RefSeq; WP_005654478.1; NC_007146.2.
DR AlphaFoldDB; Q4QMI4; -.
DR SMR; Q4QMI4; -.
DR EnsemblBacteria; AAX87763; AAX87763; NTHI0867.
DR KEGG; hit:NTHI0867; -.
DR HOGENOM; CLU_120075_1_0_6; -.
DR OMA; MGHGDDI; -.
DR OrthoDB; 1750843at2; -.
DR UniPathway; UPA00956; -.
DR Proteomes; UP000002525; 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..144
FT /note="L-fucose mutarotase"
FT /id="PRO_0000344546"
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; 15734 MW; D735520CDB792F03 CRC64;
MLKGIHPALS PELLKTLAEM GHGDEIVLAD AHFPAHSLHK NVIRADGISI DILLEAITPL
FEFDAYVDAP LLMMKAVEGD SLDPNVETRY LNAIESAVGF TPNLTSLERF DFYTRAKQAY
AVVVSGEIAK YGNIIIKKGV TPIL
