ID FUCI_BACTN Reviewed; 591 AA. AC Q9RQ13; Q7C426; DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 120. 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=BT_1273; OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50). OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=226186; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / RC VPI-5482 / E50; RX PubMed=10449780; DOI=10.1073/pnas.96.17.9833; RA Hooper L.V., Xu J., Falk P.G., Midtvedt T., Gordon J.I.; RT "A molecular sensor that allows a gut commensal to control its nutrient RT foundation in a competitive ecosystem."; RL Proc. Natl. Acad. Sci. U.S.A. 96:9833-9838(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / RC VPI-5482 / E50; RX PubMed=12663928; DOI=10.1126/science.1080029; RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., RA Hooper L.V., Gordon J.I.; RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."; RL Science 299:2074-2076(2003). CC -!- FUNCTION: Converts the aldose L-fucose into the corresponding ketose L- CC fuculose. {ECO:0000305}. 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; AF137263; AAF01484.1; -; Genomic_DNA. DR EMBL; AE015928; AAO76380.1; -; Genomic_DNA. DR RefSeq; NP_810186.1; NC_004663.1. DR RefSeq; WP_011107686.1; NC_004663.1. DR AlphaFoldDB; Q9RQ13; -. DR SMR; Q9RQ13; -. DR STRING; 226186.BT_1273; -. DR PaxDb; 226186-BT_1273; -. DR EnsemblBacteria; AAO76380; AAO76380; BT_1273. DR GeneID; 60927249; -. DR KEGG; bth:BT_1273; -. DR PATRIC; fig|226186.12.peg.1300; -. DR eggNOG; COG2407; Bacteria. DR HOGENOM; CLU_033326_1_0_10; -. DR InParanoid; Q9RQ13; -. DR OrthoDB; 9760430at2; -. DR UniPathway; UPA00563; UER00624. DR Proteomes; UP000001414; 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..591 FT /note="L-fucose isomerase" FT /id="PRO_0000204143" FT ACT_SITE 338 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254" FT ACT_SITE 362 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254" FT BINDING 338 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254" FT BINDING 362 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254" FT BINDING 529 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254" SQ SEQUENCE 591 AA; 65742 MW; 96B5874825022432 CRC64; MKKYPKIGIR PTIDGRQGGV RESLEEKTMN LAKAVAELIS NNLKNGDGSP VECIIADNTI GRVAESAACA EKFEREGVGS TITVTSCWCY GAETMDMNPH YPKAVWGFNG TERPGAVYLA AVLAGHAQKG LPAFGIYGRD VQDLDDNTIP EDVAEKILRF ARAAQAVATM RGKSYLSMGS VSMGIAGSIV NPDFFQEYLG MRNESIDLTE IIRRMEEGIY DHEEYAKAMA WTEKYCKVNE GEDFKNRPEK RKKREQKDAD WEFVVKMMII MRDLMTGNPK LKEMGFKEEA LGHNAIAAGF QGQRQWTDFY PNGDYPEALL NTSFDWNGIR EAFVVATEND ACNGVAMLFG HLLTNRAQIF SDVRTYWSPE AVKRVTGKEL TGLAANGIIH LINSGATTLD GSGQSLDAEG NPVMKEPWNL TDADVENCLK ATTWYPADRD YFRGGGFSSN FLSKGGMPVT MMRLNLIKGL GPVLQIAEGW TVEIDPEIHQ KLNMRTDPTW PTTWFVPRLC DKSAFKDVYS VMNNWGANHG AISYGHIGQD LITLASMLRI PVCMHNVDEN EIFRPTAWNA FGMDKEGADY RACTTYGPIY K //