RHAM_LEPCP
ID RHAM_LEPCP Reviewed; 106 AA.
AC B1Y3E6;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=Lcho_2208;
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Leptothrix.
OX NCBI_TaxID=395495;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) 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; CP001013; ACB34474.1; -; Genomic_DNA.
DR RefSeq; WP_012347234.1; NC_010524.1.
DR AlphaFoldDB; B1Y3E6; -.
DR SMR; B1Y3E6; -.
DR STRING; 395495.Lcho_2208; -.
DR EnsemblBacteria; ACB34474; ACB34474; Lcho_2208.
DR KEGG; lch:Lcho_2208; -.
DR eggNOG; COG3254; Bacteria.
DR HOGENOM; CLU_100689_2_0_4; -.
DR OMA; KRHDEIW; -.
DR OrthoDB; 1694303at2; -.
DR UniPathway; UPA00125; -.
DR Proteomes; UP000001693; 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; Reference proteome;
KW Rhamnose metabolism.
FT CHAIN 1..106
FT /note="L-rhamnose mutarotase"
FT /id="PRO_0000344584"
FT ACT_SITE 24
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01663"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01663"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01663"
FT BINDING 78..79
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01663"
SQ SEQUENCE 106 AA; 12291 MW; CD5B8851A855DF1E CRC64;
MTTEKIAFRM FLNPGCEAEY QLRHDRIWPE LVALLKNSGV SDYSIFLDEP RGVLFAVLSR
SPGHTMQTLP QHPVMQRWWQ HMKDIMRCNP DGSPVAEPLP CLFHLD
