ID FUCI_STRR6 Reviewed; 588 AA. AC Q8DN24; DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 117. 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}; GN OrderedLocusNames=spr1964; OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=171101; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-255 / R6; RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001; RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S., RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C., RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J., RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M., RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B., RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y., RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R., RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.; RT "Genome of the bacterium Streptococcus pneumoniae strain R6."; RL J. Bacteriol. 183:5709-5717(2001). 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; Evidence={ECO:0000255|HAMAP- CC 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 -!- 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE007317; AAL00766.1; -; Genomic_DNA. DR PIR; A99717; A99717. DR RefSeq; NP_359555.1; NC_003098.1. DR RefSeq; WP_000614258.1; NC_003098.1. DR AlphaFoldDB; Q8DN24; -. DR SMR; Q8DN24; -. DR STRING; 171101.spr1964; -. DR KEGG; spr:spr1964; -. DR PATRIC; fig|171101.6.peg.2127; -. DR eggNOG; COG2407; Bacteria. DR HOGENOM; CLU_033326_1_0_9; -. DR UniPathway; UPA00563; UER00624. DR Proteomes; UP000000586; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008790; F:arabinose isomerase activity; IBA:GO_Central. DR GO; GO:0008736; F:L-fucose isomerase activity; IBA:GO_Central. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0019571; P:D-arabinose catabolic process; IBA:GO_Central. DR GO; GO:0042355; P:L-fucose catabolic process; IBA:GO_Central. DR CDD; cd03556; L-fucose_isomerase; 1. DR Gene3D; 3.40.50.1070; -; 1. DR Gene3D; 3.20.14.10; L-fucose/L-arabinose isomerase, C-terminal; 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 NCBIfam; TIGR01089; fucI; 1. DR PANTHER; PTHR37840; L-FUCOSE ISOMERASE; 1. DR PANTHER; PTHR37840:SF1; L-FUCOSE ISOMERASE; 1. DR Pfam; PF02952; Fucose_iso_C; 1. DR Pfam; PF07881; Fucose_iso_N1; 1. DR Pfam; PF07882; Fucose_iso_N2; 1. DR SUPFAM; SSF50443; FucI/AraA C-terminal domain-like; 1. DR SUPFAM; SSF53743; FucI/AraA N-terminal and middle domains; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Cytoplasm; Fucose metabolism; Isomerase; KW Manganese; Metal-binding; Reference proteome. FT CHAIN 1..588 FT /note="L-fucose isomerase" FT /id="PRO_0000204153" FT ACT_SITE 335 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254" FT ACT_SITE 359 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254" FT BINDING 335 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254" FT BINDING 359 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254" FT BINDING 525 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254" SQ SEQUENCE 588 AA; 65850 MW; 4C114F7C5D67D559 CRC64; MIQHPRIGIR PTIDGRRQGV RESLEVQTMN MAKSVADLIS STLKYPDGEP VECVISPSTI GRVPEAAASH ELFKKSNVCA TITVTPCWCY GSETMDMSPD IPHAIWGFNG TERPGAVYLA AVLASHAQKG IPAFGIYGRD VQEASDTAIP EDVKEKLLRY ARAALATGLM RDTAYLSMGS VSMGIGGSIV NPDFFQEYLG MRNESVDMTE FTRRMDRGIY DPEEFERALK WVKENVKEGF DHNREDLVLS REEKDRQWEF VIKMFMIGRD LMVGNPRLAE LGFEEEAVGH HALVAGFQGQ RQWTDHFPNG DFMETFLNTQ FDWNGIRKPF VFATENDSLN GVSMLFNYLL TNTPQIFADV RTYWSPEAVE RVTGYTLEGR AAAGFLHLIN SGSCTLDGTG QATRDGKPVM KPFWELDESE VQAMLENTDF PPANREYFRG GGFSTRFLTK GDMPVTMVRL NLLKGVGPVL QIAEGYTLEL PEDVHHTLDN RTDPGWPTTW FAPRLTGKGA FKSVYDVMNN WGANHGAITY GHIGADLITL ASMLRIPVNM HNVPEEDIFR PKNWSLFGTE DLESADYRAC QLLGPLHK //