ID   FUCI_HAEIE              Reviewed;         589 AA.
AC   A5UAS8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
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};
GN   OrderedLocusNames=CGSHiEE_02050;
OS   Haemophilus influenzae (strain PittEE).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374930;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PittEE;
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(2007).
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; Evidence={ECO:0000255|HAMAP-
CC         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; CP000671; ABQ97879.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5UAS8; -.
DR   SMR; A5UAS8; -.
DR   KEGG; hip:CGSHiEE_02050; -.
DR   HOGENOM; CLU_033326_1_0_6; -.
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; 3.40.50.1070; -; 1.
DR   Gene3D; 3.20.14.10; L-fucose/L-arabinose isomerase, C-terminal; 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   NCBIfam; TIGR01089; fucI; 1.
DR   PANTHER; PTHR37840; L-FUCOSE ISOMERASE; 1.
DR   PANTHER; PTHR37840:SF1; L-FUCOSE ISOMERASE; 1.
DR   Pfam; PF02952; Fucose_iso_C; 1.
DR   Pfam; PF07881; Fucose_iso_N1; 1.
DR   Pfam; PF07882; Fucose_iso_N2; 1.
DR   SUPFAM; SSF50443; FucI/AraA C-terminal domain-like; 1.
DR   SUPFAM; SSF53743; FucI/AraA N-terminal and middle domains; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Fucose metabolism; Isomerase;
KW   Manganese; Metal-binding.
FT   CHAIN           1..589
FT                   /note="L-fucose isomerase"
FT                   /id="PRO_1000067221"
FT   ACT_SITE        340
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT   ACT_SITE        364
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT   BINDING         340
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT   BINDING         364
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
FT   BINDING         527
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01254"
SQ   SEQUENCE   589 AA;  65475 MW;  F1C2B26D06E2F6F1 CRC64;
     MALATQSNRI KIGIRPTIDG RRMGVRESLE TQTIRMAQSV AQLLQTHIRY TDSTFVECVV
     ADSTIGGVAE AAACADKFKR ENVGLTITVT PCWCYGSETI DMDPHMPKAI WGFNGTERPG
     AVYLAAALAG HSQLGLPAFS IYGTEVQEAD DTNIPEDVKE KLLRFARAGL AVASIRGKSY
     LSIGSVSMGI AGSIVNQAFF QEYLGMRNEY VDMMEIKRRL DRKIYDQEEV DLALSWVKQY
     CKEGVDVNSL ENQRNAEERA ELWENVVKMT IITRDLMVGN PKLATLNYAE EALGHNAIAA
     GFQGQRHWTD HLPNGDFMEA MLNSTYDWNG VRPPYILATE NDSLNAIGML FGHQLTGKAQ
     IFADVRTYWS QDSVERVTGW RPESGFIHLI NSGSAALDGT GEHQDAQGNP TLKPAWDVTE
     EEAKRCLENT RWCPAVHEYF RGGGLSSQFL TKGGIPFTMH RINLIKGLGP VLQIAEGWSI
     DLPQDVHNKL NQRTNETWPT TWFVPRLTGK GAFTDVYSVM ANWGANHCVA THGHVGADLI
     TLASMLRIPV CMHNVSEKNI FRPSAWNGFG QDKEGQDYRA CQNFGPLYK
//