FUCI_BACTN
ID FUCI_BACTN Reviewed; 591 AA.
AC Q9RQ13; Q7C426;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=BT_1273;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=10449780; DOI=10.1073/pnas.96.17.9833;
RA Hooper L.V., Xu J., Falk P.G., Midtvedt T., Gordon J.I.;
RT "A molecular sensor that allows a gut commensal to control its nutrient
RT foundation in a competitive ecosystem.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:9833-9838(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
CC -!- FUNCTION: Converts the aldose L-fucose into the corresponding ketose L-
CC fuculose. {ECO:0000305}.
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; AF137263; AAF01484.1; -; Genomic_DNA.
DR EMBL; AE015928; AAO76380.1; -; Genomic_DNA.
DR RefSeq; NP_810186.1; NC_004663.1.
DR RefSeq; WP_011107686.1; NC_004663.1.
DR AlphaFoldDB; Q9RQ13; -.
DR SMR; Q9RQ13; -.
DR STRING; 226186.BT_1273; -.
DR PaxDb; Q9RQ13; -.
DR PRIDE; Q9RQ13; -.
DR EnsemblBacteria; AAO76380; AAO76380; BT_1273.
DR GeneID; 60927249; -.
DR KEGG; bth:BT_1273; -.
DR PATRIC; fig|226186.12.peg.1300; -.
DR eggNOG; COG2407; Bacteria.
DR HOGENOM; CLU_033326_1_0_10; -.
DR InParanoid; Q9RQ13; -.
DR OMA; QDYRACA; -.
DR UniPathway; UPA00563; UER00624.
DR Proteomes; UP000001414; 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..591
FT /note="L-fucose isomerase"
FT /id="PRO_0000204143"
FT ACT_SITE 338
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT ACT_SITE 362
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT BINDING 338
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT BINDING 362
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT BINDING 529
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
SQ SEQUENCE 591 AA; 65742 MW; 96B5874825022432 CRC64;
MKKYPKIGIR PTIDGRQGGV RESLEEKTMN LAKAVAELIS NNLKNGDGSP VECIIADNTI
GRVAESAACA EKFEREGVGS TITVTSCWCY GAETMDMNPH YPKAVWGFNG TERPGAVYLA
AVLAGHAQKG LPAFGIYGRD VQDLDDNTIP EDVAEKILRF ARAAQAVATM RGKSYLSMGS
VSMGIAGSIV NPDFFQEYLG MRNESIDLTE IIRRMEEGIY DHEEYAKAMA WTEKYCKVNE
GEDFKNRPEK RKKREQKDAD WEFVVKMMII MRDLMTGNPK LKEMGFKEEA LGHNAIAAGF
QGQRQWTDFY PNGDYPEALL NTSFDWNGIR EAFVVATEND ACNGVAMLFG HLLTNRAQIF
SDVRTYWSPE AVKRVTGKEL TGLAANGIIH LINSGATTLD GSGQSLDAEG NPVMKEPWNL
TDADVENCLK ATTWYPADRD YFRGGGFSSN FLSKGGMPVT MMRLNLIKGL GPVLQIAEGW
TVEIDPEIHQ KLNMRTDPTW PTTWFVPRLC DKSAFKDVYS VMNNWGANHG AISYGHIGQD
LITLASMLRI PVCMHNVDEN EIFRPTAWNA FGMDKEGADY RACTTYGPIY K
