ID   FUCI_SALAR              Reviewed;         591 AA.
AC   A9MSA6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=SARI_04686;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-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; CP000880; ABX24450.1; -; Genomic_DNA.
DR   RefSeq; WP_000724119.1; NC_010067.1.
DR   AlphaFoldDB; A9MSA6; -.
DR   SMR; A9MSA6; -.
DR   STRING; 41514.SARI_04686; -.
DR   EnsemblBacteria; ABX24450; ABX24450; SARI_04686.
DR   KEGG; ses:SARI_04686; -.
DR   HOGENOM; CLU_033326_1_0_6; -.
DR   OMA; QDYRACA; -.
DR   OrthoDB; 507566at2; -.
DR   UniPathway; UPA00563; UER00624.
DR   Proteomes; UP000002084; 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_1000085804"
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   591 AA;  64922 MW;  DE1E289E8969258B CRC64;
     MKKISLPKIG IRPVIDGRRM GVRESLEEQT MNMAKATAAL IIEKIRHACG AQVECVIADT
     CIAGMAESAA CEEKFSSQNV GVTITVTPCW CYGSETIDMD PMRPKAIWGF NGTERPGAVY
     LAAALAAHNQ KGIPAFSIYG HDVQDADDVS IPADVEEKLL RFARAGLAVA SMKGKSYLSV
     GGVSMGIAGS IVDHNFFESW LGMKVQAVDM TELRRRIDQK IYDEAELEMA LAWADKNFRY
     GEDQNAQQYK RNEAQNRAVL KESLLMAMCI RDMMQGNKTL ADKGLVEESL GYNAIAAGFQ
     GQRHWTDQYP NGDTAEALLN SSFDWNGVRE PFIVATENDS LNGVAMLFGH QLTGTAQIFA
     DVRTYWSPEA VERVTGQALN GLAEHGIIHL INSGSAALDG ACKQRDSEGK PTMKPHWEIS
     QQEADACLAA TEWCPAIHEY FRGGGYSSRF LTEGGVPFTM TRVNMIKGLG PVLQIAEGWS
     VELPKVMHDQ LDARTNSTWP TTWFAPRLTG KGPFTDVYSV MANWGANHGV LTIGHVGADF
     ITLAAMLRIP VCMHNVEEAK IYRPSAWAAH GMDVEGQDYR ACQNYGPLYK R