RHAM_ECOLI
ID RHAM_ECOLI Reviewed; 104 AA.
AC P32156; Q2M8J8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=L-rhamnose mutarotase;
DE EC=5.1.3.32 {ECO:0000269|PubMed:15060078, ECO:0000269|PubMed:15876375};
DE AltName: Full=Rhamnose 1-epimerase;
DE AltName: Full=Type-3 mutarotase;
GN Name=rhaM; Synonyms=yiiL; OrderedLocusNames=b3901, JW3872;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15060078; DOI=10.1074/jbc.m402016200;
RA Ryu K.-S., Kim C., Kim I., Yoo S., Choi B.-S., Park C.;
RT "NMR application probes a novel and ubiquitous family of enzymes that alter
RT monosaccharide configuration.";
RL J. Biol. Chem. 279:25544-25548(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH L-RHAMNOSE, CATALYTIC
RP ACTIVITY, SUBUNIT, MUTAGENESIS OF TYR-18, AND REACTION MECHANISM.
RX PubMed=15876375; DOI=10.1016/j.jmb.2005.03.047;
RA Ryu K.-S., Kim J.-I., Cho S.-J., Park D., Park C., Cheong H.-K., Lee J.-O.,
RA Choi B.-S.;
RT "Structural insights into the monosaccharide specificity of Escherichia
RT coli rhamnose mutarotase.";
RL J. Mol. Biol. 349:153-162(2005).
CC -!- FUNCTION: Involved in the anomeric conversion of L-rhamnose.
CC {ECO:0000269|PubMed:15060078}.
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:0000269|PubMed:15060078, ECO:0000269|PubMed:15876375};
CC -!- PATHWAY: Carbohydrate metabolism; L-rhamnose metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15876375}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the rhamnose mutarotase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L19201; AAB03034.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76883.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77408.1; -; Genomic_DNA.
DR PIR; S40845; S40845.
DR RefSeq; NP_418337.1; NC_000913.3.
DR RefSeq; WP_000619493.1; NZ_SSZK01000026.1.
DR PDB; 1X8D; X-ray; 1.80 A; A/B/C/D=1-104.
DR PDBsum; 1X8D; -.
DR AlphaFoldDB; P32156; -.
DR SMR; P32156; -.
DR BioGRID; 4262642; 28.
DR IntAct; P32156; 2.
DR STRING; 511145.b3901; -.
DR PaxDb; P32156; -.
DR PRIDE; P32156; -.
DR EnsemblBacteria; AAC76883; AAC76883; b3901.
DR EnsemblBacteria; BAE77408; BAE77408; BAE77408.
DR GeneID; 948402; -.
DR KEGG; ecj:JW3872; -.
DR KEGG; eco:b3901; -.
DR PATRIC; fig|1411691.4.peg.2805; -.
DR EchoBASE; EB1811; -.
DR eggNOG; COG3254; Bacteria.
DR HOGENOM; CLU_100689_2_0_6; -.
DR InParanoid; P32156; -.
DR OMA; KRHDEIW; -.
DR PhylomeDB; P32156; -.
DR BioCyc; EcoCyc:EG11865-MON; -.
DR BioCyc; MetaCyc:EG11865-MON; -.
DR BRENDA; 5.1.3.32; 2026.
DR UniPathway; UPA00125; -.
DR EvolutionaryTrace; P32156; -.
DR PRO; PR:P32156; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0062192; F:L-rhamnose mutarotase activity; IDA:EcoCyc.
DR GO; GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; IBA:GO_Central.
DR GO; GO:0019301; P:rhamnose catabolic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Isomerase;
KW Reference proteome; Rhamnose metabolism.
FT CHAIN 1..104
FT /note="L-rhamnose mutarotase"
FT /id="PRO_0000169687"
FT ACT_SITE 22
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT BINDING 18
FT /ligand="substrate"
FT BINDING 41
FT /ligand="substrate"
FT BINDING 76..77
FT /ligand="substrate"
FT MUTAGEN 18
FT /note="Y->F: Loss of mutarotase activity."
FT /evidence="ECO:0000269|PubMed:15876375"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:1X8D"
FT HELIX 15..20
FT /evidence="ECO:0007829|PDB:1X8D"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:1X8D"
FT HELIX 27..35
FT /evidence="ECO:0007829|PDB:1X8D"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:1X8D"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:1X8D"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:1X8D"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:1X8D"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:1X8D"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:1X8D"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1X8D"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1X8D"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:1X8D"
SQ SEQUENCE 104 AA; 12265 MW; 6A276C08E0EEC7E2 CRC64;
MIRKAFVMQV NPDAHEEYQR RHNPIWPELE AVLKSHGAHN YAIYLDKARN LLFAMVEIES
EERWNAVAST DVCQRWWKYM TDVMPANPDN SPVSSELQEV FYLP
