FUCI_STRR6
ID FUCI_STRR6 Reviewed; 588 AA.
AC Q8DN24;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=spr1964;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
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; AE007317; AAL00766.1; -; Genomic_DNA.
DR PIR; A99717; A99717.
DR RefSeq; NP_359555.1; NC_003098.1.
DR RefSeq; WP_000614258.1; NC_003098.1.
DR AlphaFoldDB; Q8DN24; -.
DR SMR; Q8DN24; -.
DR STRING; 171101.spr1964; -.
DR EnsemblBacteria; AAL00766; AAL00766; spr1964.
DR GeneID; 60234008; -.
DR KEGG; spr:spr1964; -.
DR PATRIC; fig|171101.6.peg.2127; -.
DR eggNOG; COG2407; Bacteria.
DR HOGENOM; CLU_033326_1_0_9; -.
DR OMA; QDYRACA; -.
DR UniPathway; UPA00563; UER00624.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008790; F:arabinose isomerase activity; IBA:GO_Central.
DR GO; GO:0008736; F:L-fucose isomerase activity; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019571; P:D-arabinose catabolic process; IBA:GO_Central.
DR GO; GO:0042355; P:L-fucose catabolic process; IBA:GO_Central.
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..588
FT /note="L-fucose isomerase"
FT /id="PRO_0000204153"
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; 65850 MW; 4C114F7C5D67D559 CRC64;
MIQHPRIGIR PTIDGRRQGV RESLEVQTMN MAKSVADLIS STLKYPDGEP VECVISPSTI
GRVPEAAASH ELFKKSNVCA TITVTPCWCY GSETMDMSPD IPHAIWGFNG TERPGAVYLA
AVLASHAQKG IPAFGIYGRD VQEASDTAIP 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
