ID   FUCI_CLOPE              Reviewed;         595 AA.
AC   Q8XNL5;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=CPE0318;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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}.
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DR   EMBL; BA000016; BAB80024.1; -; Genomic_DNA.
DR   RefSeq; WP_011009734.1; NC_003366.1.
DR   AlphaFoldDB; Q8XNL5; -.
DR   SMR; Q8XNL5; -.
DR   STRING; 195102.gene:10489574; -.
DR   EnsemblBacteria; BAB80024; BAB80024; BAB80024.
DR   KEGG; cpe:CPE0318; -.
DR   HOGENOM; CLU_033326_1_0_9; -.
DR   OMA; QDYRACA; -.
DR   UniPathway; UPA00563; UER00624.
DR   Proteomes; UP000000818; 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..595
FT                   /note="L-fucose isomerase"
FT                   /id="PRO_0000204144"
FT   ACT_SITE        341
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT   ACT_SITE        365
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT   BINDING         341
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT   BINDING         365
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT   BINDING         531
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
SQ   SEQUENCE   595 AA;  65929 MW;  D37D1B6FAB3D169B CRC64;
     MKTYPKIGIR PTIDGRQGGV RESLEEKAMK MAQAAKKLIE NSLYYADGTP VQCVLASRTI
     GGSGDAGIVQ QEFTGKNIVA TLSVTPSWCY GTETMDLDPN TIKAIWGFNG TERPGAVYLA
     AAMSGYAQKG IPAFKIYGHD VQELDDDTIP VDVQEKILSF ARGAIAVGQM KGKSYVNIGA
     SSMGIAGSQV DISFFEDYLG MLVEFVDMTE ILRRIHLEIF DPIEYDKALN WIKENCREGI
     DINEGKDLPD IVKKSKVIPA DKDWEFIAKQ AIIIRDILYR NEKLGDLGWE EEARGRNAIA
     GGFQGQRQWT DWLPNGDFTE AIMASTFDWN GPRQVTAFAT ENDTLNGVSM LLGTLLTNKA
     PIFSDVRTYW SPESVKRVTG KELTGKAKNG IIHLINSGAS ALDGTAAAKD KDGNKTMKEF
     WNMTNEDVQS CLKATDWCRA NYEYFRGGGF SSHFKTEAEL PVTLIRVNLI KGIGPTLQIA
     EGYTCVIDED IHQILDERTD KTWPTTWFAP NLGECGFETV YDVMNHWGAN HGAFVHGHIG
     SDLITLASML RIPVTLHNVP RERIFRPNIF EGAGTKALET ADFEICRLLG PLYKK