RHAM_RHILT
ID RHAM_RHILT Reviewed; 106 AA.
AC Q7BSH1;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=L-rhamnose mutarotase;
DE EC=5.1.3.32 {ECO:0000269|PubMed:18156270};
DE AltName: Full=Rhamnose 1-epimerase;
DE AltName: Full=Type-3 mutarotase;
GN Name=rhaM; Synonyms=rhaU;
OS Rhizobium leguminosarum bv. trifolii.
OG Plasmid pRleW14-2c.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=386;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=Rlt100;
RX PubMed=15576793; DOI=10.1128/jb.186.24.8433-8442.2004;
RA Richardson J.S., Hynes M.F., Oresnik I.J.;
RT "A genetic locus necessary for rhamnose uptake and catabolism in Rhizobium
RT leguminosarum bv. trifolii.";
RL J. Bacteriol. 186:8433-8442(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH L-RHAMNOSE, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVE SITE, REACTION MECHANISM, SUBUNIT, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Rlt100;
RX PubMed=18156270; DOI=10.1128/jb.01120-07;
RA Richardson J.S., Carpena X., Switala J., Perez-Luque R., Donald L.J.,
RA Loewen P.C., Oresnik I.J.;
RT "RhaU of Rhizobium leguminosarum is a rhamnose mutarotase.";
RL J. Bacteriol. 190:2903-2910(2008).
CC -!- FUNCTION: Involved in the anomeric conversion of L-rhamnose.
CC {ECO:0000269|PubMed:18156270}.
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:18156270};
CC -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation.
CC {ECO:0000269|PubMed:15576793}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18156270}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the rhamnose mutarotase family. {ECO:0000305}.
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DR EMBL; AF085687; AAQ92411.1; -; Genomic_DNA.
DR PDB; 2QLW; X-ray; 1.60 A; A/B=2-106.
DR PDB; 2QLX; X-ray; 2.00 A; A/B=1-106.
DR PDBsum; 2QLW; -.
DR PDBsum; 2QLX; -.
DR AlphaFoldDB; Q7BSH1; -.
DR SMR; Q7BSH1; -.
DR BioCyc; MetaCyc:MON-18536; -.
DR BRENDA; 5.1.3.32; 5343.
DR UniPathway; UPA00541; -.
DR EvolutionaryTrace; Q7BSH1; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0062192; F:L-rhamnose mutarotase activity; IEA:UniProtKB-EC.
DR GO; GO:0019301; P:rhamnose catabolic process; IEA:UniProtKB-UniPathway.
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; Plasmid;
KW Rhamnose metabolism.
FT CHAIN 1..106
FT /note="L-rhamnose mutarotase"
FT /id="PRO_0000344593"
FT ACT_SITE 24
FT /note="Proton donor"
FT BINDING 20
FT /ligand="substrate"
FT BINDING 43
FT /ligand="substrate"
FT BINDING 78..79
FT /ligand="substrate"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:2QLW"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:2QLW"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:2QLW"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:2QLW"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:2QLW"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:2QLW"
FT HELIX 66..71
FT /evidence="ECO:0007829|PDB:2QLW"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:2QLW"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2QLW"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:2QLW"
SQ SEQUENCE 106 AA; 12292 MW; 4DE860C3A622C7F5 CRC64;
MTLEKHAFKM QLNPGMEAEY RKRHDEIWPE LVDLLHQSGA SDYSIHLDRE TNTLFGVLTR
PKDHTMASLP DHPVMKKWWA HMADIMATNP DNSPVQSDLV TLFHMP