FUCI_BACFR
ID FUCI_BACFR Reviewed; 590 AA.
AC Q64ZS4;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=BF0253;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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; AP006841; BAD47002.1; -; Genomic_DNA.
DR RefSeq; WP_005779363.1; NC_006347.1.
DR RefSeq; YP_097536.1; NC_006347.1.
DR AlphaFoldDB; Q64ZS4; -.
DR SMR; Q64ZS4; -.
DR STRING; 295405.BF0253; -.
DR EnsemblBacteria; BAD47002; BAD47002; BF0253.
DR GeneID; 66330667; -.
DR KEGG; bfr:BF0253; -.
DR PATRIC; fig|295405.11.peg.283; -.
DR HOGENOM; CLU_033326_1_0_10; -.
DR OMA; QDYRACA; -.
DR UniPathway; UPA00563; UER00624.
DR Proteomes; UP000002197; 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..590
FT /note="L-fucose isomerase"
FT /id="PRO_0000204142"
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 590 AA; 65341 MW; 043D6B2AAED8DD0D CRC64;
MKKYPKIGIR PTIDGRQGGV RESLEEKTMN LAKAVAELIT SNLKNGDGTP VECVIADGTI
GRVAESAACA EKFEREGVGA TITVTSCWCY GAETMDMNPY YPKAVWGFNG TERPGAVYLA
AVLAGHAQKG LPAFGIYGRD VQDLNDNSIP ADVAEKILRF ARAAQAVATM RGKSYLSMGS
VSMGIAGSIV NPDFFQEYLG MRNESIDLTE IIRRMAEGIY DKEEYAKAMA WTEKYCKKNE
GNDFNIPEKT KTRAQKDEDW EFIVKMTIIM RDLMQGNPKL KELGFKEEAL GHNAIAAGFQ
GQRQWTDFYP NGDFSEALLN TSFDWNGIRE AFVVATENDA CNGVAMLFGH LLTNRAQIFS
DVRTYWSPEA VKRVTGKELT GMAANGIIHL INSGATTLDG TGQQTNANGE PAMKPCWEIT
EGEVEKCLEA TTWYPANRDY FRGGGFSSNF LSKGGMPVTM MRLNLIKGLG PVLQIAEGWT
VEIDPEIHKL LDERTDRTWP TTWFVPRLCD KPAFKDVYSV MNNWGANHGA ISYGHIGQDV
ITLASMLRIP VCMHNVEEDQ IFRPAAWNAF GMDKEGADYR ACTTYGPIYK
