FUCM_ECOLI
ID FUCM_ECOLI Reviewed; 140 AA.
AC P0AEN8; P11555; Q2MA30; Q46923;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=L-fucose mutarotase;
DE EC=5.1.3.29 {ECO:0000269|PubMed:15060078, ECO:0000269|PubMed:19524593};
DE AltName: Full=D-ribose pyranase;
DE EC=5.4.99.62 {ECO:0000269|PubMed:15060078, ECO:0000269|PubMed:19524593};
DE AltName: Full=Fucose 1-epimerase;
DE AltName: Full=Type-2 mutarotase;
GN Name=fucU; OrderedLocusNames=b2804, JW2775;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2664711; DOI=10.1093/nar/17.12.4883;
RA Lu Z., Lin E.C.C.;
RT "The nucleotide sequence of Escherichia coli genes for L-fucose
RT dissimilation.";
RL Nucleic Acids Res. 17:4883-4884(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP SUBUNIT.
RX PubMed=12738765; DOI=10.1074/jbc.m304523200;
RA Kim M.-S., Shin J., Lee W., Lee H.-S., Oh B.-H.;
RT "Crystal structures of RbsD leading to the identification of cytoplasmic
RT sugar-binding proteins with a novel folding architecture.";
RL J. Biol. Chem. 278:28173-28180(2003).
RN [5]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=15060078; DOI=10.1074/jbc.m402016200;
RA Ryu K.-S., Kim C., Kim I., Yoo S., Choi B.-S., Park C.;
RT "NMR application probes a novel and ubiquitous family of enzymes that alter
RT monosaccharide configuration.";
RL J. Biol. Chem. 279:25544-25548(2004).
RN [6] {ECO:0007744|PDB:2WCV}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH L-FUCOSE, SUBUNIT,
RP SUBSTRATE-BINDING SITES, ACTIVE SITE, MUTAGENESIS OF HIS-22; ASP-64 AND
RP TYR-111, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=19524593; DOI=10.1016/j.jmb.2009.06.022;
RA Lee K.H., Ryu K.S., Kim M.S., Suh H.Y., Ku B., Song Y.L., Ko S., Lee W.,
RA Oh B.H.;
RT "Crystal structures and enzyme mechanisms of a dual fucose
RT mutarotase/ribose pyranase.";
RL J. Mol. Biol. 391:178-191(2009).
CC -!- FUNCTION: Involved in the anomeric conversion of L-fucose. Catalyzes
CC also the interconversion of beta-pyran and beta-furan forms of D-
CC ribose. {ECO:0000269|PubMed:15060078, ECO:0000269|PubMed:19524593}.
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:0000269|PubMed:15060078, ECO:0000269|PubMed:19524593};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-ribopyranose = beta-D-ribofuranose;
CC Xref=Rhea:RHEA:25432, ChEBI:CHEBI:27476, ChEBI:CHEBI:47002;
CC EC=5.4.99.62; Evidence={ECO:0000269|PubMed:15060078,
CC ECO:0000269|PubMed:19524593};
CC -!- PATHWAY: Carbohydrate metabolism; L-fucose metabolism.
CC {ECO:0000269|PubMed:15060078, ECO:0000269|PubMed:19524593}.
CC -!- SUBUNIT: Homodecamer. {ECO:0000269|PubMed:12738765,
CC ECO:0000269|PubMed:19524593}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RbsD / FucU family. FucU mutarotase
CC subfamily. {ECO:0000305}.
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DR EMBL; X15025; CAA33129.1; -; Genomic_DNA.
DR EMBL; U29581; AAB40454.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75846.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76876.1; -; Genomic_DNA.
DR PIR; H65062; Q4ECKR.
DR RefSeq; NP_417284.1; NC_000913.3.
DR RefSeq; WP_000920840.1; NZ_STEB01000030.1.
DR PDB; 2WCV; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J=1-140.
DR PDBsum; 2WCV; -.
DR AlphaFoldDB; P0AEN8; -.
DR SMR; P0AEN8; -.
DR BioGRID; 4262305; 18.
DR DIP; DIP-47990N; -.
DR IntAct; P0AEN8; 5.
DR STRING; 511145.b2804; -.
DR jPOST; P0AEN8; -.
DR PaxDb; P0AEN8; -.
DR PRIDE; P0AEN8; -.
DR EnsemblBacteria; AAC75846; AAC75846; b2804.
DR EnsemblBacteria; BAE76876; BAE76876; BAE76876.
DR GeneID; 66673329; -.
DR GeneID; 945842; -.
DR KEGG; ecj:JW2775; -.
DR KEGG; eco:b2804; -.
DR PATRIC; fig|511145.12.peg.2904; -.
DR EchoBASE; EB0350; -.
DR eggNOG; COG4154; Bacteria.
DR HOGENOM; CLU_120075_1_0_6; -.
DR InParanoid; P0AEN8; -.
DR OMA; MGHGDDI; -.
DR PhylomeDB; P0AEN8; -.
DR BioCyc; EcoCyc:EG10355-MON; -.
DR BioCyc; MetaCyc:EG10355-MON; -.
DR BRENDA; 5.1.3.29; 2026.
DR BRENDA; 5.4.99.62; 2026.
DR UniPathway; UPA00956; -.
DR EvolutionaryTrace; P0AEN8; -.
DR PRO; PR:P0AEN8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; ISS:EcoCyc.
DR GO; GO:0062193; F:D-ribose pyranase activity; IEA:UniProtKB-EC.
DR GO; GO:0042806; F:fucose binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0036373; F:L-fucose mutarotase activity; IDA:EcoCyc.
DR GO; GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; IDA:EcoCyc.
DR GO; GO:0006004; P:fucose metabolic process; IBA:GO_Central.
DR GO; GO:0036065; P:fucosylation; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Fucose metabolism;
KW Isomerase; Reference proteome.
FT CHAIN 1..140
FT /note="L-fucose mutarotase"
FT /id="PRO_0000087380"
FT ACT_SITE 22
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:19524593"
FT ACT_SITE 64
FT /evidence="ECO:0000269|PubMed:19524593"
FT ACT_SITE 111
FT /evidence="ECO:0000269|PubMed:19524593"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19524593"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19524593"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19524593"
FT BINDING 129..131
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19524593"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19524593"
FT MUTAGEN 22
FT /note="H->A: Affects slightly binding affinity toward L-
FT fucose. Significantly reduced ribose pyranase activity."
FT /evidence="ECO:0000269|PubMed:19524593"
FT MUTAGEN 64
FT /note="D->A: Affects slightly binding affinity toward L-
FT fucose. Significantly reduced ribose pyranase activity."
FT /evidence="ECO:0000269|PubMed:19524593"
FT MUTAGEN 111
FT /note="Y->F: Reduces binding affinity toward L-fucose.
FT Significantly reduced ribose pyranase activity."
FT /evidence="ECO:0000269|PubMed:19524593"
FT CONFLICT 106..140
FT /note="NRFAFYERAQKAFAIVITGERAKYGNILLKKGVTP -> IVLRFMNGRKKPL
FT RSLSQANERSTGIFF (in Ref. 1; CAA33129)"
FT /evidence="ECO:0000305"
FT HELIX 11..19
FT /evidence="ECO:0007829|PDB:2WCV"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:2WCV"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:2WCV"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:2WCV"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:2WCV"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:2WCV"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:2WCV"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:2WCV"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:2WCV"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:2WCV"
FT HELIX 107..114
FT /evidence="ECO:0007829|PDB:2WCV"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:2WCV"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:2WCV"
SQ SEQUENCE 140 AA; 15473 MW; 55D304F7BF17B8F4 CRC64;
MLKTISPLIS PELLKVLAEM GHGDEIIFSD AHFPAHSMGP QVIRADGLLV SDLLQAIIPL
FELDSYAPPL VMMAAVEGDT LDPEVERRYR NALSLQAPCP DIIRINRFAF YERAQKAFAI
VITGERAKYG NILLKKGVTP
