ID   RHAA_ENTFA              Reviewed;         428 AA.
AC   Q838L2;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=EF_0434;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
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   -!- 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; AE016830; AAO80290.1; -; Genomic_DNA.
DR   RefSeq; NP_814219.1; NC_004668.1.
DR   RefSeq; WP_002387675.1; NZ_KE136524.1.
DR   AlphaFoldDB; Q838L2; -.
DR   SMR; Q838L2; -.
DR   STRING; 226185.EF_0434; -.
DR   EnsemblBacteria; AAO80290; AAO80290; EF_0434.
DR   KEGG; efa:EF0434; -.
DR   PATRIC; fig|226185.45.peg.2899; -.
DR   eggNOG; COG4806; Bacteria.
DR   HOGENOM; CLU_052790_0_0_9; -.
DR   OMA; HKVNLHA; -.
DR   UniPathway; UPA00541; UER00601.
DR   Proteomes; UP000001415; 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; Reference proteome;
KW   Rhamnose metabolism.
FT   CHAIN           1..428
FT                   /note="L-rhamnose isomerase"
FT                   /id="PRO_0000090555"
FT   BINDING         260
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00541"
FT   BINDING         292
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"
SQ   SEQUENCE   428 AA;  48923 MW;  E554829445C2263A CRC64;
     MTTITQKYEE AKEKYASIDV DTEAVLEKMA DVKISMHVWQ GDDVRGFLSE DELSGGISVT
     GNYPGVARSP QQLRQDLEKA FSLIPGKHKL NLHAIYLDTE ERVDLNELEP KHFEPWVTWA
     KENGLGLDFN PTFFSHPMYR DGFTLAHPNP QVRDFWIEHG KRSRRIAEYF GRELGQVAVN
     NFWVPDGFKD NPVDRLTPRK RLMASLDEIF SEEIDPAYTV DAMESKLFGI GSEAYTVGSH
     EFYMGYGLTR NKLICLDAGH FHPTEVISNK LSSLSLFGEG MLLHVSRPVR WDSDHVVIMD
     DELQEIAKEL VRNDLLGKTH VGLDFFDATI NRVAAWVIGT RNTQKALMKA MLEPTNVLKE
     AELIGDFTTR LALTEELKDF PFADIWNYYC QENHVPIGLD WLTDVQEYEK VILPTRQLPT
     GKDSCRFS