ID   FUCI_SALTI              Reviewed;         591 AA.
AC   Q8Z429; Q7C7H4;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   03-AUG-2022, entry version 115.
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=STY3116, t2884;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO70440.1; Type=Erroneous termination; Note=Truncated C-terminus. However, it could be a natural mutation leading to a slightly truncated protein.; Evidence={ECO:0000305};
CC       Sequence=CAD02802.1; Type=Erroneous termination; Note=Truncated C-terminus. However, it could be a natural mutation leading to a slightly truncated protein.; Evidence={ECO:0000305};
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DR   EMBL; AL513382; CAD02802.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AE014613; AAO70440.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; NP_457371.1; NC_003198.1.
DR   AlphaFoldDB; Q8Z429; -.
DR   SMR; Q8Z429; -.
DR   STRING; 220341.16504056; -.
DR   EnsemblBacteria; AAO70440; AAO70440; t2884.
DR   KEGG; stt:t2884; -.
DR   KEGG; sty:STY3116; -.
DR   PATRIC; fig|220341.7.peg.3171; -.
DR   eggNOG; COG2407; Bacteria.
DR   HOGENOM; CLU_033326_1_0_6; -.
DR   OMA; QDYRACA; -.
DR   UniPathway; UPA00563; UER00624.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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.
FT   CHAIN           1..591
FT                   /note="L-fucose isomerase"
FT                   /id="PRO_0000204149"
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;  64797 MW;  EEDC132F04F5AD98 CRC64;
     MKKISLPKIG IRPVIDGRRM GVRESLEEQT MNMAKATAAL ITEKIRHACG AQVECVIADT
     CIAGMAESAA CEEKFSSQNV GVTITVTPCW CYGSETIDMD PMRPKAIWGF NGTERPGAVY
     LAAALAAHSQ KGIPAFSIYG HDVQDADDTS IPADVEEKLL RFARAGLAVA SMKGKSYLSV
     GGVSMGIAGS IVDHNFFESW LGMKVQAVDM TELRRRIDQK IYDEAELEMA LAWADKNFRY
     GEDQNASQYK RNEAQNRAVL KESLLMAMCI RDMMQGNKTL ADKGLVEESL GYNAIAAGFQ
     GQRHWTDQYP NGDTAEALLN SSFDWNGVRE PFVVATENDS LNGVAMLFGH QLTGTAQIFA
     DVRTYWSPEA VERVTGQALS ALAEHGIIHL INSGSAALDG ACKQRDSEGK PTMKPHWEIS
     QQEADACLAA TEWCPAIHEY FRGGGYSSRF LTEGGVPFTM TRVNIIKGLG PVLQIAEGWS
     VELPKAMHDQ LDARTNSTWP TTWFAPRLIG KGPFTDVYSV MANWGANHGV LTIGHVGADF
     ITLAAMLRIP VCMHNVEEAK IYRPSAWAAH GMDIEGQDYR ACQNYGPLYK R