ID   RHAM_ECO24              Reviewed;         104 AA.
AC   A7ZUB2;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
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};
GN   OrderedLocusNames=EcE24377A_4432;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV17851.1; -; Genomic_DNA.
DR   RefSeq; WP_000619503.1; NC_009801.1.
DR   AlphaFoldDB; A7ZUB2; -.
DR   BMRB; A7ZUB2; -.
DR   SMR; A7ZUB2; -.
DR   EnsemblBacteria; ABV17851; ABV17851; EcE24377A_4432.
DR   GeneID; 66672190; -.
DR   KEGG; ecw:EcE24377A_4432; -.
DR   HOGENOM; CLU_100689_2_0_6; -.
DR   OMA; KRHDEIW; -.
DR   UniPathway; UPA00125; -.
DR   Proteomes; UP000001122; 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..104
FT                   /note="L-rhamnose mutarotase"
FT                   /id="PRO_0000344573"
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   104 AA;  12235 MW;  6A34F1BE281EC7E2 CRC64;
     MIRKAFVMQV NPDAHEEYQR RHNPIWPELE AVLKSHGAHN YAIYLDKARN LLFATVEIES
     EERWNAVAST DVCQRWWKYM TDVMPANPDN SPVSSELQEV FYLP