ID FUCI_ECOL5 Reviewed; 591 AA. AC Q0TE57; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-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=ECP_2785; OS Escherichia coli O6:K15:H31 (strain 536 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=362663; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x; RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.; RT "Role of pathogenicity island-associated integrases in the genome RT plasticity of uropathogenic Escherichia coli strain 536."; RL Mol. Microbiol. 61:584-595(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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000247; ABG70772.1; -; Genomic_DNA. DR RefSeq; YP_670673.1; -. DR SMR; Q0TE57; 1-591. DR GeneID; 4189103; -. DR GenomeReviews; CP000247_GR; ECP_2785. DR KEGG; ecp:ECP_2785; -. DR NMPDR; fig|340197.3.peg.1265; -. DR HOGENOM; Q0TE57; -. DR OMA; Q0TE57; TWFVPRL. DR BioCyc; ECOL362663:ECP_2785-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_1000067219. 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; 65004 MW; 9A3A1906AEBC7718 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 QLTGTAQIFA DVRTYWSPEA IERVTGHKLD GLAEHGIIHL INSGSAALDG SCKQRDSEGK PTMKPHWEIS QQEADACLAA TEWCPAIHEY FRGGGYSSRF LTEGGVPFTM TRVNIIKGLG PVLQIAEGWS VELPKDVHDI LNKRTNSTWP TTWFAPRLTG KGPFTDVYSV MANWGANHGV LTIGHVGADF ITLASMLRIP VCMHNVEETK VYRPSAWAAH GMDIEGQDYR ACQNYGPLYK R //