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RHAM_BURCA
ID   RHAM_BURCA              Reviewed;         104 AA.
AC   Q1BGJ2;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Bcen_6401;
OS   Burkholderia cenocepacia (strain AU 1054).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=331271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU 1054;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., LiPuma J.J., Konstantinidis K.,
RA   Tiedje J.M., Richardson P.;
RT   "Complete sequence of chromosome 3 of Burkholderia cenocepacia AU 1054.";
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000380; ABF81263.1; -; Genomic_DNA.
DR   RefSeq; WP_011549798.1; NC_008062.1.
DR   AlphaFoldDB; Q1BGJ2; -.
DR   SMR; Q1BGJ2; -.
DR   EnsemblBacteria; ABF81263; ABF81263; Bcen_6401.
DR   KEGG; bcn:Bcen_6401; -.
DR   HOGENOM; CLU_100689_2_0_4; -.
DR   OMA; KRHDEIW; -.
DR   UniPathway; UPA00125; -.
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_0000344557"
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;  12281 MW;  484C119EC46BBFD6 CRC64;
     METIAFRMHL HPGKRDEYRR RHDAIWPELA DALRAAGISD YWIFLDDDTH HLFAVLKRPA
     DHRIAQLAET DVMRRWWAYM ADLMATGPDG RPVEKALEPM FHLE
 
 
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