ID   RHAA_SALPA              Reviewed;         419 AA.
AC   Q5PKG4;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=SPA3889;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV79655.1; -; Genomic_DNA.
DR   RefSeq; WP_000211468.1; NC_006511.1.
DR   AlphaFoldDB; Q5PKG4; -.
DR   SMR; Q5PKG4; -.
DR   EnsemblBacteria; AAV79655; AAV79655; SPA3889.
DR   KEGG; spt:SPA3889; -.
DR   HOGENOM; CLU_052790_0_0_6; -.
DR   OMA; HKVNLHA; -.
DR   UniPathway; UPA00541; UER00601.
DR   Proteomes; UP000008185; 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_0000090564"
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;  47397 MW;  9F3BB87DC9F77BFB CRC64;
     MTTQLEQAWE LAKQRFAAVG IDVEEALRQL DRLPVSMHCW QGDDVAGFEN PEGSLTGGIQ
     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 ARLALLEEQK SLPWQAVWEM YCQRHDTPAG SQWLDSVRAY EKEILSKRS