RHAM_LIGS1
ID RHAM_LIGS1 Reviewed; 108 AA.
AC Q1WRE3;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, 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}; OrderedLocusNames=LSL_1753;
OS Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OG Plasmid pMP118.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=362948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCC118;
RX PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT "Multireplicon genome architecture of Lactobacillus salivarius.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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; CP000234; ABE00555.1; -; Genomic_DNA.
DR RefSeq; WP_003699292.1; NC_007930.1.
DR RefSeq; YP_536638.1; NC_007930.1.
DR AlphaFoldDB; Q1WRE3; -.
DR SMR; Q1WRE3; -.
DR EnsemblBacteria; ABE00555; ABE00555; LSL_1753.
DR KEGG; lsl:LSL_1753; -.
DR PATRIC; fig|362948.14.peg.1858; -.
DR HOGENOM; CLU_100689_2_0_9; -.
DR OMA; KRHDEIW; -.
DR UniPathway; UPA00125; -.
DR Proteomes; UP000006559; Plasmid pMP118.
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-UniPathway.
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; Plasmid; Reference proteome;
KW Rhamnose metabolism.
FT CHAIN 1..108
FT /note="L-rhamnose mutarotase"
FT /id="PRO_0000344583"
FT ACT_SITE 23
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01663"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01663"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01663"
FT BINDING 80..81
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01663"
SQ SEQUENCE 108 AA; 12670 MW; 5478238E35E069B7 CRC64;
MTVRLGQIMH VNPNYYDEYE KRHSDLPVKF PEMKKALKEA GAHNYSIYLD KKTGTLFAYL
EVDDMDKYKA IAEMDACKEW WAYMAPLMDT NPDKSPVTFD LPEVFHLD
