ID   RHAA_SALTY              Reviewed;         419 AA.
AC   P27031;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2001, sequence version 2.
DT   03-AUG-2022, entry version 128.
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=STM4046;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-70.
RC   STRAIN=LT2;
RX   PubMed=1657713; DOI=10.1016/0378-1119(91)90511-9;
RA   Nishitani J., Wilcox G.;
RT   "Cloning and characterization of the L-rhamnose regulon in Salmonella
RT   typhimurium LT2.";
RL   Gene 105:37-42(1991).
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}.
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; AE006468; AAL22886.1; -; Genomic_DNA.
DR   EMBL; X57299; CAA40558.1; -; Genomic_DNA.
DR   PIR; S21854; S21854.
DR   RefSeq; NP_462927.1; NC_003197.2.
DR   RefSeq; WP_000211470.1; NC_003197.2.
DR   AlphaFoldDB; P27031; -.
DR   SMR; P27031; -.
DR   STRING; 99287.STM4046; -.
DR   PaxDb; P27031; -.
DR   EnsemblBacteria; AAL22886; AAL22886; STM4046.
DR   GeneID; 1255573; -.
DR   KEGG; stm:STM4046; -.
DR   PATRIC; fig|99287.12.peg.4263; -.
DR   HOGENOM; CLU_052790_0_0_6; -.
DR   PhylomeDB; P27031; -.
DR   BioCyc; SENT99287:STM4046-MON; -.
DR   UniPathway; UPA00541; UER00601.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008740; F:L-rhamnose isomerase activity; IBA:GO_Central.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019324; P:L-lyxose metabolic process; IBA:GO_Central.
DR   GO; GO:0019301; P:rhamnose catabolic process; IBA:GO_Central.
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; Reference proteome;
KW   Rhamnose metabolism.
FT   CHAIN           1..419
FT                   /note="L-rhamnose isomerase"
FT                   /id="PRO_0000090566"
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"
FT   CONFLICT        60..70
FT                   /note="QSTGNYPGKAR -> RNHGHSCFLCE (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   419 AA;  47425 MW;  9F3BAAF6C9F77BFB 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 SQWLDSVRVY EKEILSKRS