ID   RHAM_SHIBS              Reviewed;          99 AA.
AC   Q31U88;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=L-rhamnose mutarotase {ECO:0000255|HAMAP-Rule:MF_01663};
DE            EC=5.1.3.32 {ECO:0000255|HAMAP-Rule:MF_01663};
DE   AltName: Full=Rhamnose 1-epimerase {ECO:0000255|HAMAP-Rule:MF_01663};
DE   AltName: Full=Type-3 mutarotase {ECO:0000255|HAMAP-Rule:MF_01663};
GN   Name=rhaM {ECO:0000255|HAMAP-Rule:MF_01663}; OrderedLocusNames=SBO_3919;
OS   Shigella boydii serotype 4 (strain Sb227).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300268;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sb227;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Involved in the anomeric conversion of L-rhamnose.
CC       {ECO:0000255|HAMAP-Rule:MF_01663}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-L-rhamnose = beta-L-rhamnose; Xref=Rhea:RHEA:25584,
CC         ChEBI:CHEBI:27586, ChEBI:CHEBI:27907; EC=5.1.3.32;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01663};
CC   -!- PATHWAY: Carbohydrate metabolism; L-rhamnose metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_01663}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01663}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01663}.
CC   -!- SIMILARITY: Belongs to the rhamnose mutarotase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01663}.
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DR   EMBL; CP000036; ABB68370.1; -; Genomic_DNA.
DR   RefSeq; WP_000619504.1; NC_007613.1.
DR   AlphaFoldDB; Q31U88; -.
DR   SMR; Q31U88; -.
DR   EnsemblBacteria; ABB68370; ABB68370; SBO_3919.
DR   KEGG; sbo:SBO_3919; -.
DR   HOGENOM; CLU_100689_2_0_6; -.
DR   OMA; KRHDEIW; -.
DR   UniPathway; UPA00125; -.
DR   Proteomes; UP000007067; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0062192; F:L-rhamnose mutarotase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019299; P:rhamnose metabolic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01663; L_rham_rotase; 1.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR013448; L-rhamnose_mutarotase.
DR   InterPro; IPR008000; Rham/fucose_mutarotase.
DR   Pfam; PF05336; rhaM; 1.
DR   SUPFAM; SSF54909; SSF54909; 1.
DR   TIGRFAMs; TIGR02625; YiiL_rotase; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Isomerase; Rhamnose metabolism.
FT   CHAIN           1..99
FT                   /note="L-rhamnose mutarotase"
FT                   /id="PRO_0000344604"
FT   ACT_SITE        22
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01663"
FT   BINDING         18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01663"
FT   BINDING         41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01663"
FT   BINDING         76..77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01663"
SQ   SEQUENCE   99 AA;  11543 MW;  1DA7E214FD298BD6 CRC64;
     MIRKAFVMQV NPDAHEEYQR RHNPIWPELE AVLKSHGAHN YAIYLDKARN LLFATVEIES
     EERWNAVAST DVCQRWWKYM TDVMPANPDN SPVSSELQG