ID   FUCI_PHOV8              Reviewed;         591 AA.
AC   A6L048;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=BVU_1373;
OS   Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 /
OS   NBRC 14291 / NCTC 11154) (Bacteroides vulgatus).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Phocaeicola.
OX   NCBI_TaxID=435590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC
RC   11154;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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;
CC         Evidence={ECO:0000255|HAMAP-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; CP000139; ABR39062.1; -; Genomic_DNA.
DR   RefSeq; WP_005849650.1; NC_009614.1.
DR   AlphaFoldDB; A6L048; -.
DR   SMR; A6L048; -.
DR   STRING; 435590.BVU_1373; -.
DR   PRIDE; A6L048; -.
DR   EnsemblBacteria; ABR39062; ABR39062; BVU_1373.
DR   GeneID; 56614942; -.
DR   KEGG; bvu:BVU_1373; -.
DR   eggNOG; COG2407; Bacteria.
DR   HOGENOM; CLU_033326_1_0_10; -.
DR   OMA; QDYRACA; -.
DR   OrthoDB; 507566at2; -.
DR   BioCyc; BVUL435590:G1G59-1434-MON; -.
DR   UniPathway; UPA00563; UER00624.
DR   Proteomes; UP000002861; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0042355; P:L-fucose catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.14.10; -; 1.
DR   Gene3D; 3.40.275.10; -; 1.
DR   Gene3D; 3.40.50.1070; -; 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   Pfam; PF02952; Fucose_iso_C; 1.
DR   Pfam; PF07881; Fucose_iso_N1; 1.
DR   Pfam; PF07882; Fucose_iso_N2; 1.
DR   SUPFAM; SSF50443; SSF50443; 1.
DR   SUPFAM; SSF53743; SSF53743; 1.
DR   TIGRFAMs; TIGR01089; fucI; 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_1000067214"
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;  65620 MW;  4FDDE43BE6329449 CRC64;
     MKKYPKIGIR PTIDGRQGGV RESLEDKTMN LAKAVAELIS SNLKNGDGSP VECVIADSTI
     GRVAESAACA EKFEREGVGA TITVTSCWCY GSETMDMHPH WPKAVWGFNG TERPGAVYLA
     AVLAGHAQKG LPAFGIYGHD VQDLDDNTIP ADVAEKLLRF ARAAMAVANM RGKSYLSFGS
     VCMGIAGSIV DPDFFQEYLG IRNESVDETE ILRRMEEGIY DHEEYAKAMA WTEKYCKPNE
     GEDFKNRPEK RKTREEKDAD WEFIVKMTII MRDLMVGNPK LLEMGFKEEA IGHNAIAAGF
     QGQRQWTDWK PNGDFSEALL NTTFDWNGIR EAYVLATEND ACNGVAMLFG HLLSGCGQMF
     SDIRTYWSPE AVKRVTGKEL TGMAKNGIIH LINSGATTLD ATGESHNEAG EPCMKPNWEM
     TEADVEACLK ATTWYPADRD YFRGGGFSSN FLSKGGMPVT MMRLNLVKGL GPVLQLAEGW
     TVDIDPEIHQ VLNMRTDPTW PTTWFVPRLC DKPAFRDVYS VMNNWGANHG AISYGHIGQD
     LITLASMLRI PVCMHNVEDD KIFRPASWNA FGMDKEGSDY RACSTYGPIY K