ID   RHAM_SALPK              Reviewed;         104 AA.
AC   B5BJG3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=SSPA3614;
OS   Salmonella paratyphi A (strain AKU_12601).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=554290;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AKU_12601;
RX   PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA   Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA   Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA   Mungall K., Dougan G., Parkhill J.;
RT   "Pseudogene accumulation in the evolutionary histories of Salmonella
RT   enterica serovars Paratyphi A and Typhi.";
RL   BMC Genomics 10:36-36(2009).
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; FM200053; CAR61896.1; -; Genomic_DNA.
DR   RefSeq; WP_000619478.1; NC_011147.1.
DR   AlphaFoldDB; B5BJG3; -.
DR   SMR; B5BJG3; -.
DR   KEGG; sek:SSPA3614; -.
DR   HOGENOM; CLU_100689_2_0_6; -.
DR   OMA; KRHDEIW; -.
DR   UniPathway; UPA00125; -.
DR   Proteomes; UP000001869; 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_1000187231"
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;  12334 MW;  CBF4810E83A5C217 CRC64;
     MIRKAFVMQV NADAHEEYQR RHNPIWPELE AVLKSHGAHH YAIYLDQERN LLFATVEIES
     EERWNAVAST DVCQRWWKHM RDVMPANPDN SPVSAELKEV FYLQ