ID FUCI_SHIF8 Reviewed; 591 AA. AC Q0T157; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 23. 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=SFV_2881; OS Shigella flexneri serotype 5b (strain 8401). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=373384; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16822325; DOI=10.1186/1471-2164-7-173; RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., RA Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., RA Jin Q.; RT "Complete genome sequence of Shigella flexneri 5b and comparison with RT Shigella flexneri 2a."; RL BMC Genomics 7:173-173(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; CP000266; ABF04958.1; -; Genomic_DNA. DR RefSeq; YP_690263.1; -. DR SMR; Q0T157; 1-591. DR GeneID; 4210301; -. DR GenomeReviews; CP000266_GR; SFV_2881. DR KEGG; sfv:SFV_2881; -. DR HOGENOM; Q0T157; -. DR OMA; Q0T157; TWFVPRL. DR BioCyc; SFLE373384:SFV_2881-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_1000067226. 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; 64977 MW; E6245DEEDF34EF9B 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 SSFDWNGVRE PFVVATENDS LNGVAMLMGH QLTGTAQVFA DVRTYWSPEA IERVTGHKLD GLAEHGIIHL INSGSAALDG SCKQRDSEGN PTMKPHWEIS QQEADACLAA TEWCPAIHEY FRGGGYSSRF LTEGGVPFTM TRVNIIKGLG PVLQIAEGWS VELPKDVHDI LNKRTNSTWP TTWFAPRLTG KGPFTDVYSV MANWGANHGV LTIGHVGADF ITLASMLRIP VCMHNVEETK VYRPSAWAAH GMDIEGQDYR ACQNYGPLYK R //