RHAA_YERPP
ID RHAA_YERPP Reviewed; 418 AA.
AC A4TRT1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=L-rhamnose isomerase {ECO:0000255|HAMAP-Rule:MF_00541};
DE EC=5.3.1.14 {ECO:0000255|HAMAP-Rule:MF_00541};
GN Name=rhaA {ECO:0000255|HAMAP-Rule:MF_00541}; OrderedLocusNames=YPDSF_3643;
OS Yersinia pestis (strain Pestoides F).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=386656;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pestoides F;
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 Di Bartolo G., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Worsham P., Chu M., Bearden S., Garcia E.,
RA Richardson P.;
RT "Complete sequence of chromosome of Yersinia pestis Pestoides F.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of L-rhamnose and L-rhamnulose.
CC {ECO:0000255|HAMAP-Rule:MF_00541}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-rhamnopyranose = L-rhamnulose; Xref=Rhea:RHEA:23160,
CC ChEBI:CHEBI:17897, ChEBI:CHEBI:62346; EC=5.3.1.14;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00541};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00541};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00541};
CC -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation; glycerone
CC phosphate from L-rhamnose: step 1/3. {ECO:0000255|HAMAP-Rule:MF_00541}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00541}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00541}.
CC -!- SIMILARITY: Belongs to the rhamnose isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00541}.
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DR EMBL; CP000668; ABP41993.1; -; Genomic_DNA.
DR RefSeq; WP_002209104.1; NZ_CP009715.1.
DR AlphaFoldDB; A4TRT1; -.
DR SMR; A4TRT1; -.
DR PRIDE; A4TRT1; -.
DR GeneID; 57974276; -.
DR KEGG; ypp:YPDSF_3643; -.
DR PATRIC; fig|386656.14.peg.305; -.
DR OMA; HKVNLHA; -.
DR UniPathway; UPA00541; UER00601.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008740; F:L-rhamnose isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019301; P:rhamnose catabolic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_00541; RhaA; 1.
DR InterPro; IPR009308; Rhamnose_isomerase.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR Pfam; PF06134; RhaA; 1.
DR SUPFAM; SSF51658; SSF51658; 1.
DR TIGRFAMs; TIGR01748; rhaA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Isomerase; Manganese; Metal-binding; Rhamnose metabolism.
FT CHAIN 1..418
FT /note="L-rhamnose isomerase"
FT /id="PRO_1000017726"
FT BINDING 262
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00541"
FT BINDING 294
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00541"
FT BINDING 296
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00541"
SQ SEQUENCE 418 AA; 47160 MW; C4267475B767A79E CRC64;
MTNSIEQAWD LAKQRFAAVG VDVDAALTRL DTLPVSMHCW QGDDVTGFED PDGVLTGGIQ
ATGNYPGKAR NATELRSDLE LALALIPGPK RLNLHAIYLE SDTPVARNKI EPRHFSHWVA
WAKKHQLGLD FNPSCFSHPL SADGFTLSHA DPEIRQFWIE HCQASRRVSA YFGEQLGTPS
VMNIWIPDGM KDTPIDRLAP RQRLLSALDE VISEKLNPAH HIDAVESKLF GIGAESYTVG
SNEFYMGYAA SRQTALCLDA GHFHPTEVIS DKISSAMLYV PRLLLHVSRP VRWDSDHVVL
LDDETQAIAS EIIRHNLFDR VHIGLDFFDA SINRIAAWVI GTRNMKKALL RALLEPTDRL
RQLELRGDYT ARLALLEEQK SLPWQAIWEG YCQRNDVPVD ARWLDAVREY EQQILSQR