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FUCM_HISS2
ID   FUCM_HISS2              Reviewed;         144 AA.
AC   B0US22;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=L-fucose mutarotase {ECO:0000255|HAMAP-Rule:MF_01662};
DE            EC=5.1.3.29 {ECO:0000255|HAMAP-Rule:MF_01662};
DE   AltName: Full=Fucose 1-epimerase {ECO:0000255|HAMAP-Rule:MF_01662};
DE   AltName: Full=Type-2 mutarotase {ECO:0000255|HAMAP-Rule:MF_01662};
GN   Name=fucU {ECO:0000255|HAMAP-Rule:MF_01662}; OrderedLocusNames=HSM_0581;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the anomeric conversion of L-fucose.
CC       {ECO:0000255|HAMAP-Rule:MF_01662}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-L-fucose = beta-L-fucose; Xref=Rhea:RHEA:25580,
CC         ChEBI:CHEBI:42548, ChEBI:CHEBI:42589; EC=5.1.3.29;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01662};
CC   -!- PATHWAY: Carbohydrate metabolism; L-fucose metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_01662}.
CC   -!- SUBUNIT: Homodecamer. {ECO:0000255|HAMAP-Rule:MF_01662}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01662}.
CC   -!- SIMILARITY: Belongs to the RbsD / FucU family. FucU mutarotase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01662}.
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DR   EMBL; CP000947; ACA32233.1; -; Genomic_DNA.
DR   RefSeq; WP_012341412.1; NC_010519.1.
DR   AlphaFoldDB; B0US22; -.
DR   SMR; B0US22; -.
DR   STRING; 228400.HSM_0581; -.
DR   EnsemblBacteria; ACA32233; ACA32233; HSM_0581.
DR   GeneID; 56965493; -.
DR   KEGG; hsm:HSM_0581; -.
DR   HOGENOM; CLU_120075_1_0_6; -.
DR   OMA; MGHGDDI; -.
DR   OrthoDB; 1750843at2; -.
DR   UniPathway; UPA00956; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042806; F:fucose binding; IEA:InterPro.
DR   GO; GO:0036373; F:L-fucose mutarotase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042354; P:L-fucose metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1650.10; -; 1.
DR   HAMAP; MF_01662; L_fucose_rotase; 1.
DR   InterPro; IPR023751; L-fucose_mutarotase.
DR   InterPro; IPR023750; RbsD-like_sf.
DR   InterPro; IPR007721; RbsD_FucU.
DR   Pfam; PF05025; RbsD_FucU; 1.
DR   SUPFAM; SSF102546; SSF102546; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Fucose metabolism; Isomerase.
FT   CHAIN           1..144
FT                   /note="L-fucose mutarotase"
FT                   /id="PRO_1000187186"
FT   ACT_SITE        22
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01662"
FT   BINDING         30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01662"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01662"
FT   BINDING         131..133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01662"
SQ   SEQUENCE   144 AA;  15756 MW;  1D34E69CD84720C1 CRC64;
     MLKGIHPAIS PDLLKILAEM GHGDELVLSD AHFPAHQLHH KVVRADGISI NSLLTGITPL
     FEFDTYTEAP LIMMQAVEGD SLDPAVEQSY LQTIKSAVGN VPKLARMDRF AFYERAKQAY
     AVVITGETAK YGNIIIKKGV TPVK
 
 
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