ID FUCI_BACFN Reviewed; 590 AA. AC Q5LIN8; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2005, sequence version 1. DT 04-NOV-2026, entry version 116. 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=BF0211; OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 OS / LMG 10263 / NCTC 9343 / Onslow / VPI 2553 / EN-2). OC Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales; OC Bacteroidaceae; Bacteroides. OX NCBI_TaxID=272559; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / LMG 10263 / RC NCTC 9343 / Onslow / VPI 2553 / EN-2; RX PubMed=15746427; DOI=10.1126/science.1107008; RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V., RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A., RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A., RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J., RA Barrell B.G., Parkhill J.; RT "Extensive DNA inversions in the B. fragilis genome control variable gene RT expression."; RL Science 307:1463-1465(2005). 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; CR626927; CAH05988.1; -; Genomic_DNA. DR RefSeq; WP_010991938.1; NC_003228.3. DR AlphaFoldDB; Q5LIN8; -. DR SMR; Q5LIN8; -. DR GeneID; 60367857; -. DR KEGG; bfs:BF9343_0209; -. DR eggNOG; COG2407; Bacteria. DR HOGENOM; CLU_033326_1_0_10; -. DR OMA; AACMEKF; -. DR UniPathway; UPA00563; UER00624. DR Proteomes; UP000006731; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008790; F:arabinose isomerase activity; IEA:TreeGrafter. 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:0019571; P:D-arabinose catabolic process; IEA:TreeGrafter. DR GO; GO:0042355; P:L-fucose catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd03556; L-fucose_isomerase; 1. DR FunFam; 3.20.14.10:FF:000001; L-fucose isomerase; 1. DR FunFam; 3.40.275.10:FF:000001; L-fucose isomerase; 1. DR FunFam; 3.40.50.1070:FF:000001; L-fucose isomerase; 1. DR Gene3D; 3.40.50.1070; -; 1. DR Gene3D; 3.40.275.10; L-fucose Isomerase, Chain A, domain 2; 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 NCBIfam; NF008220; PRK10991.1; 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..590 FT /note="L-fucose isomerase" FT /id="PRO_1000067213" 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 590 AA; 65371 MW; 058D6B26DFD8DD08 CRC64; MKKYPKIGIR PTIDGRQGGV RESLEEKTMN LAKAVAELIT SNLKNGDGTP VECVIADGTI GRVAESAACA EKFEREGVGA TITVTSCWCY GAETMDMNPY YPKAVWGFNG TERPGAVYLA AVLAGHAQKG LPAFGIYGRD VQDLNDNSIP ADVAEKILRF ARAAQAVATM RGKSYLSMGS VSMGIAGSIV NPDFFQEYLG MRNESIDLTE IIRRMAEGIY DKEEYAKAMA WTEKYCKKNE GNDFNIPEKT KTRAQKDEDW EFIVKMTIIM RDLMQGNPKL KELGFKEEAL GHNAIAAGFQ GQRQWTDFYP NGDFSEALLN TSFDWNGIRE AFVVTTENDA CNGVAMLFGH LLTNRAQIFS DVRTYWSPEA VKRVTGKELT GMAANGIIHL INSGATTLDG TGQQTNANGE PAMKPCWEIT EGEVEKCLEA TTWYPANRDY FRGGGFSSNF LSKGGMPVTM MRLNLIKGLG PVLQIAEGWT VEIDPEIHKL LDERTDRTWP TTWFVPRLCD KPAFKDVYSV MNNWGANHGA ISYGHIGQDV ITLASMLRIP VCMHNVEEDQ IFRPAAWNAF GMDKEGADYR ACTTYGPIYK //