ID   RHAA_SALG2              Reviewed;         419 AA.
AC   B5RFC5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=SG3375;
OS   Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=287/91 / NCTC 13346;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(2008).
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; AM933173; CAR39168.1; -; Genomic_DNA.
DR   RefSeq; WP_000211482.1; NC_011274.1.
DR   AlphaFoldDB; B5RFC5; -.
DR   SMR; B5RFC5; -.
DR   EnsemblBacteria; CAR39168; CAR39168; SG3375.
DR   KEGG; seg:SG3375; -.
DR   HOGENOM; CLU_052790_0_0_6; -.
DR   OMA; HKVNLHA; -.
DR   UniPathway; UPA00541; UER00601.
DR   Proteomes; UP000008321; Chromosome.
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..419
FT                   /note="L-rhamnose isomerase"
FT                   /id="PRO_1000128889"
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   419 AA;  47544 MW;  F66227D334C39FCE CRC64;
     MTTQLEQAWE LAKQRFAAVG IDVEEALRQL DRLPVSMHCW QGDDVAGFEN REGSLTGGIQ
     STGNYPGKAR NATELRADLE QALRLIPGPK RLNLHAIYLE SDTPVARDQI KPEHFKNWVE
     WAKANRLGLD FNPTCFSHPL SADGFTLSHP DAKIRQFWID HCKASRRVSA YFGEQLGTPS
     VMNIWIPDGM KDITVDRLAP RQRLLEALDE VISEKFDPAH HIDAVESKLF GIGAESYTVG
     SNEFYMGYAT SRQTALCLDA GHFHPTEVIS DKISAAMLYV PRLLLHVSRP VRWDSDHVVL
     LDDETQAIAS EIVRHNLFDR VHIGLDFFDA SINRVAAWVI GTRNMKKALL RALLEPTDQL
     RQLEASGDYT VRLALLEEQK SLPWQAVWEM YCQRHDTPTG SQWLDSVRTY EKEILSKRS