FUCI_STRZT
ID FUCI_STRZT Reviewed; 588 AA.
AC C1CU77;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=SPT_2171;
OS Streptococcus pneumoniae (strain Taiwan19F-14).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=487213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Taiwan19F-14;
RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA Rappuoli R., Moxon E.R., Masignani V.;
RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT closely related species.";
RL Genome Biol. 11:R107.1-R107.19(2010).
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; CP000921; ACO22340.1; -; Genomic_DNA.
DR RefSeq; WP_000614263.1; NC_012469.1.
DR AlphaFoldDB; C1CU77; -.
DR SMR; C1CU77; -.
DR KEGG; snt:SPT_2171; -.
DR HOGENOM; CLU_033326_1_0_9; -.
DR OMA; QDYRACA; -.
DR UniPathway; UPA00563; UER00624.
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..588
FT /note="L-fucose isomerase"
FT /id="PRO_1000165101"
FT ACT_SITE 335
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT ACT_SITE 359
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT BINDING 335
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT BINDING 359
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT BINDING 525
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
SQ SEQUENCE 588 AA; 65739 MW; 04AD1B8F2E13E420 CRC64;
MIQHPRIGIR PTIDGRRQGV RESLEVQTMN MAKSVADLIS STLKYPDGEP VECVISPSTI
GRVPEAAASH ELFKKSNVCA TITVTPCWCY GSETMDMSPD IPHAIWGFNG TERPGAVYLA
AVLASHAQKG IPAFGIYGRD VQEASDTAIP EDVKEKLLRY ARAALATGLM RDTAYLSMGS
VSMGIGGSIV NPDFFQEYLG MRNESVDMTE FTRRMDRGIY DPEEFERAMV WVKEHIKEGV
DRNREDLILS KEEKEKQWEF VIKMFMIGRD LMVGNPRLAE LGFEEEAVGH HALVAGFQGQ
RQWTDHFPNG DFMETFLNTQ FDWNGIRKPF VFATENDSLN GVSMLFNYLL TNTPQIFADV
RTYWSPEAVK RVTGHTLEGC AAAGFLHLIN SGSCTLDGTG QATRDGKPVM KPFWELDESE
VQAMLENTDF PPANREYFRG GGFSTRFLTK GDMPVTMVRL NLLKGVGPVL QIAEGYTLEL
PEDVHHTLDN RTDPGWPTTW FAPRLTGKGA FKSVYDVMNN WGANHGAITY GHIGADLITL
ASMLRIPVNM HNVPEEDIFR PKNWSLFGTE DLESADYRAC QLLGPLHK