RHAM_ECOLC
ID RHAM_ECOLC Reviewed; 104 AA.
AC B1IVH7;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=EcolC_4116;
OS Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS WDCM 00012 / Crooks).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=481805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Ingram L., Richardson P.;
RT "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL Submitted (FEB-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; CP000946; ACA79714.1; -; Genomic_DNA.
DR RefSeq; WP_000619493.1; NZ_CP022959.1.
DR AlphaFoldDB; B1IVH7; -.
DR BMRB; B1IVH7; -.
DR SMR; B1IVH7; -.
DR KEGG; ecl:EcolC_4116; -.
DR HOGENOM; CLU_100689_2_0_6; -.
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_0000344569"
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; 12265 MW; 6A276C08E0EEC7E2 CRC64;
MIRKAFVMQV NPDAHEEYQR RHNPIWPELE AVLKSHGAHN YAIYLDKARN LLFAMVEIES
EERWNAVAST DVCQRWWKYM TDVMPANPDN SPVSSELQEV FYLP