FUCI_STRZP
ID FUCI_STRZP Reviewed; 588 AA.
AC C1CND0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=SPP_2209;
OS Streptococcus pneumoniae (strain P1031).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=488223;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1031;
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; CP000920; ACO21786.1; -; Genomic_DNA.
DR RefSeq; WP_000614270.1; NC_012467.1.
DR AlphaFoldDB; C1CND0; -.
DR SMR; C1CND0; -.
DR KEGG; spp:SPP_2209; -.
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_1000165100"
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; 65907 MW; 29B6BC574FDB07D9 CRC64;
MIQHPRIGIR PTIDGRRQGV RESLEVQTMN MAKSVADLIS STLKYPDGEP VECVISPSTI
GRVPEAAASH ELFKKSNVCA TITVTPCWCY GSETMDMSPD IPHAIWGFNG TERPGAVYLA
AVLASHTQKG IPAFGIYGRD VQEANDTAIP EDVKEKLLRY ARAALATGLM RDTAYLSMGS
VSMGIGGSIV NPDFFQEYLG MRNESVDMTE FTRRMDRGIY DPEEFERALK WVKENVKEGF
DHNREDLVLS REEKDRQWEF VIKMFMIGRD LMVGNPRLAE LGFEEEAVGH HALVAGFQGQ
RQWTDHFPNG DFMETFLNTQ FDWNGIRKPF VFATENDSLN GVSMLFNYLL TNTPQIFADV
RTYWSPEAVE RVTGYTLEGR AAAGFLHLIN SGSCTLDGTG QATRDGKPVM KPFWELDESE
VQAMLENTDF PPANREYFRG GGFSTRFLTK GDMPVTMVRL NLLKGVGPVL QIAEGYTLEL
PEDVHHTLDN RTDPGWPTTW FAPRLTGKGA FKSVYDVMNN WGANHGAITY GHIGADLITL
ASMLRIPVNM HNVPEEDIFR PKNWSLFGTE DLESADYRAC QLLGPLHK