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   16-JUN-2009, entry version 25.
DE   RecName: Full=L-fucose isomerase;
DE            EC=5.3.1.25;
DE   AltName: Full=6-deoxy-L-galactose isomerase;
DE   AltName: Full=FucIase;
GN   Name=fucI; OrderedLocusNames=UTI89_C3174;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.,
RA   Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA   Hultgren S.J., Gordon J.I.;
RT   "Identification of genes subject to positive selection in
RT   uropathogenic strains of Escherichia coli: a comparative genomics
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- FUNCTION: Converts the aldose L-fucose into the corresponding
CC       ketose L-fuculose (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-fucose = L-fuculose.
CC   -!- COFACTOR: Manganese (By similarity).
CC   -!- PATHWAY: Carbohydrate degradation; L-fucose degradation; L-
CC       lactaldehyde and glycerone phosphate from L-fucose: step 1/3.
CC   -!- SUBUNIT: Homohexamer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the L-fucose isomerase family.
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DR   EMBL; CP000243; ABE08626.1; -; Genomic_DNA.
DR   RefSeq; YP_542157.1; -.
DR   SMR; Q1R7N8; 1-591.
DR   GeneID; 3990309; -.
DR   GenomeReviews; CP000243_GR; UTI89_C3174.
DR   KEGG; eci:UTI89_C3174; -.
DR   HOGENOM; Q1R7N8; -.
DR   OMA; Q1R7N8; TWFVPRL.
DR   BioCyc; ECOL364106:UTI89_C3174-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008736; F:L-fucose isomerase activity; IEA:HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019317; P:fucose catabolic process; IEA:InterPro.
DR   HAMAP; MF_01254; -; 1.
DR   InterPro; IPR015888; Fuc_isomerase-like_C.
DR   InterPro; IPR004216; Fuc_isomerase_C.
DR   InterPro; IPR012888; Fucose_iso_N1.
DR   InterPro; IPR005763; Fucose_isomerase.
DR   InterPro; IPR012889; Fucose_isomerase_N2.
DR   Gene3D; G3DSA:3.20.14.10; Fuc_isomerase_C; 1.
DR   Gene3D; G3DSA:3.40.50.1070; Fucose_iso_N1; 1.
DR   Gene3D; G3DSA:3.40.275.10; Fucose_iso_N2; 1.
DR   Pfam; PF02952; Fucose_iso_C; 1.
DR   Pfam; PF07881; Fucose_iso_N1; 1.
DR   Pfam; PF07882; Fucose_iso_N2; 1.
DR   TIGRFAMs; TIGR01089; fucI; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Complete proteome; Cytoplasm;
KW   Fucose metabolism; Isomerase; Manganese; Metal-binding.
FT   CHAIN         1    591       L-fucose isomerase.
FT                                /FTId=PRO_1000067220.
FT   ACT_SITE    337    337       Proton acceptor (By similarity).
FT   ACT_SITE    361    361       Proton acceptor (By similarity).
FT   METAL       337    337       Manganese (By similarity).
FT   METAL       361    361       Manganese (By similarity).
FT   METAL       528    528       Manganese (By similarity).
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
//