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RHAM_ECOL5
ID   RHAM_ECOL5              Reviewed;         104 AA.
AC   Q0TAG2;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=ECP_4111;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(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; CP000247; ABG72067.1; -; Genomic_DNA.
DR   RefSeq; WP_000619492.1; NC_008253.1.
DR   AlphaFoldDB; Q0TAG2; -.
DR   SMR; Q0TAG2; -.
DR   STRING; 362663.ECP_4111; -.
DR   EnsemblBacteria; ABG72067; ABG72067; ECP_4111.
DR   KEGG; ecp:ECP_4111; -.
DR   HOGENOM; CLU_100689_2_0_6; -.
DR   OMA; KRHDEIW; -.
DR   UniPathway; UPA00125; -.
DR   Proteomes; UP000009182; 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_0000344577"
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;  12190 MW;  DC589BA4281EC7F3 CRC64;
     MIRKAFVMQV NPDAHEEYQR RHNPIWPELE AVLKSHGAHN YAIYLDKAHN LLFATVEIES
     EERWNAVAST DVCQRWWKYM TDVMPANADN SPVSSELQEV FYLP
 
 
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