ID   FUCI_ECOUT              Reviewed;         591 AA.
AC   Q1R7N8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=L-fucose isomerase {ECO:0000255|HAMAP-Rule:MF_01254};
DE            EC=5.3.1.25 {ECO:0000255|HAMAP-Rule:MF_01254};
DE   AltName: Full=6-deoxy-L-galactose isomerase {ECO:0000255|HAMAP-Rule:MF_01254};
DE   AltName: Full=FucIase;
GN   Name=fucI {ECO:0000255|HAMAP-Rule:MF_01254}; OrderedLocusNames=UTI89_C3174;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- FUNCTION: Converts the aldose L-fucose into the corresponding ketose L-
CC       fuculose. {ECO:0000255|HAMAP-Rule:MF_01254}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-fucose = L-fuculose; Xref=Rhea:RHEA:17233, ChEBI:CHEBI:2181,
CC         ChEBI:CHEBI:17617; EC=5.3.1.25; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01254};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01254};
CC   -!- PATHWAY: Carbohydrate degradation; L-fucose degradation; L-lactaldehyde
CC       and glycerone phosphate from L-fucose: step 1/3. {ECO:0000255|HAMAP-
CC       Rule:MF_01254}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01254}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01254}.
CC   -!- SIMILARITY: Belongs to the L-fucose isomerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01254}.
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DR   EMBL; CP000243; ABE08626.1; -; Genomic_DNA.
DR   RefSeq; WP_000724161.1; NC_007946.1.
DR   AlphaFoldDB; Q1R7N8; -.
DR   SMR; Q1R7N8; -.
DR   EnsemblBacteria; ABE08626; ABE08626; UTI89_C3174.
DR   KEGG; eci:UTI89_C3174; -.
DR   HOGENOM; CLU_033326_1_0_6; -.
DR   OMA; QDYRACA; -.
DR   UniPathway; UPA00563; UER00624.
DR   Proteomes; UP000001952; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008736; F:L-fucose isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042355; P:L-fucose catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.14.10; -; 1.
DR   Gene3D; 3.40.275.10; -; 1.
DR   Gene3D; 3.40.50.1070; -; 1.
DR   HAMAP; MF_01254; Fucose_iso; 1.
DR   InterPro; IPR004216; Fuc/Ara_isomerase_C.
DR   InterPro; IPR038393; Fuc_iso_dom3_sf.
DR   InterPro; IPR015888; Fuc_isomerase_C.
DR   InterPro; IPR038391; Fucose_iso_dom1_sf.
DR   InterPro; IPR012888; Fucose_iso_N1.
DR   InterPro; IPR005763; Fucose_isomerase.
DR   InterPro; IPR038392; Fucose_isomerase_dom2_sf.
DR   InterPro; IPR009015; Fucose_isomerase_N/cen_sf.
DR   InterPro; IPR012889; Fucose_isomerase_N2.
DR   Pfam; PF02952; Fucose_iso_C; 1.
DR   Pfam; PF07881; Fucose_iso_N1; 1.
DR   Pfam; PF07882; Fucose_iso_N2; 1.
DR   SUPFAM; SSF50443; SSF50443; 1.
DR   SUPFAM; SSF53743; SSF53743; 1.
DR   TIGRFAMs; TIGR01089; fucI; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Fucose metabolism; Isomerase;
KW   Manganese; Metal-binding.
FT   CHAIN           1..591
FT                   /note="L-fucose isomerase"
FT                   /id="PRO_1000067220"
FT   ACT_SITE        337
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT   ACT_SITE        361
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT   BINDING         337
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT   BINDING         361
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT   BINDING         528
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
SQ   SEQUENCE   591 AA;  64990 MW;  E1519E4EDA35128E CRC64;
     MKKISLPKIG IRPVIDGRRM GVRESLEEQT MNMAKATAAL LTEKLRHACG AAVECVISDT
     CIAGMAEAAA CEEKFSSQNV GLTITVTPCW CYGSETIDMD PTRPKAIWGF NGTERPGAVY
     LAAALAAHSQ KGIPAFSIYG HDVQDADDTS IPADVEEKLL RFARAGLAVA SMKGKSYLSL
     GGVSMGIAGS IVDHNFFESW LGMKVQAVDM TELRRRIDQK IYDEAELEMA LAWADKNFRY
     GEDENNKQYQ RNAEQSRAVL RESLLMAMCI RDMMQGNSKL ADIGRVEESL GYNAIAAGFQ
     GQRHWTDQYP NGDTAEAILN SSFDWNGVRK PFVVATENDS LNGVAMLMGH QLTGTAQVFA
     DVRTYWSPEA IERVTGHKLD GLAEHGIIHL INSGSAALDG SCKQRDSEGK PTMKPHWEIS
     QQEADACLAA TEWCPAIHEY FRGGGYSSRF LTEGGVPFTM TRVNIIKGLG PVLQIAEGWS
     VELPKDVHDI LNKRTNSTWP TTWFAPRLTG KGPFTDVYSV MANWGANHGV LTIGHVGADF
     ITLASMLRIP VCMHNVEETK VYRPSAWAAH GMDIEGQDYR ACQNYGPLYK R