ID   RHAA_BACTN              Reviewed;         418 AA.
AC   Q8A1A2;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   07-JAN-2015, entry version 76.
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};
GN   OrderedLocusNames=BT_3764;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC
OS   10582 / E50 / VPI-5482).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K.,
RA   Chiang H.C., Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
CC   -!- CATALYTIC ACTIVITY: L-rhamnopyranose = L-rhamnulose.
CC       {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-
CC       Rule:MF_00541};
CC   -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation;
CC       glycerone phosphate from L-rhamnose: step 1/3. {ECO:0000255|HAMAP-
CC       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; AE015928; AAO78869.1; -; Genomic_DNA.
DR   RefSeq; NP_812675.1; NC_004663.1.
DR   ProteinModelPortal; Q8A1A2; -.
DR   SMR; Q8A1A2; 6-418.
DR   STRING; 226186.BT_3764; -.
DR   EnsemblBacteria; AAO78869; AAO78869; BT_3764.
DR   GeneID; 1076390; -.
DR   KEGG; bth:BT_3764; -.
DR   PATRIC; 21062537; VBIBacThe70966_3826.
DR   eggNOG; COG4806; -.
DR   HOGENOM; HOG000269679; -.
DR   InParanoid; Q8A1A2; -.
DR   KO; K01813; -.
DR   OMA; ISLHCWQ; -.
DR   OrthoDB; EOG6KMB74; -.
DR   BioCyc; BTHE226186:GJXV-3832-MONOMER; -.
DR   UniPathway; UPA00541; UER00601.
DR   Proteomes; UP000001414; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008740; F:L-rhamnose isomerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019301; P:rhamnose catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.150; -; 1.
DR   HAMAP; MF_00541; RhaA; 1.
DR   InterPro; IPR009308; Rhamnose_isomerase.
DR   InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR   Pfam; PF06134; RhaA; 1.
DR   SUPFAM; SSF51658; SSF51658; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Isomerase; Manganese; Metal-binding;
KW   Reference proteome; Rhamnose metabolism.
FT   CHAIN         1    418       L-rhamnose isomerase.
FT                                /FTId=PRO_0000090551.
FT   METAL       262    262       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00541}.
FT   METAL       294    294       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00541}.
FT   METAL       296    296       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00541}.
SQ   SEQUENCE   418 AA;  47482 MW;  EFC25B788F3BC353 CRC64;
     MKKEEMIQKA YEIAVERYAA VGVDTEKVLK TMQDFHLSLH CWQADDVTGF EVQAGALSGG
     IQATGNYPGK ARNIDELRAD ILKAASYIPG THRLNLHEIY GDFQGKVVDR DQVEPEHFKS
     WIEWGKEHNM KLDFNSTSFS HPKSGDLSLS NPDEGIRQFW IEHTKRCRAV AEEMGKAQGD
     PCIMNLWVHD GSKDITVNRM KYRALLKDSL DQIFATEYKN MKDCIESKVF GIGLESYTVG
     SNDFYIGYGA SRNKMVTLDT GHFHPTESVA DKVSSLLLYV PELMLHVSRP VRWDSDHVTI
     MDDPTMELFS EIVRCGALER VHYGLDYFDA SINRIGAYVI GSRAAQKCMT RALLEPIAKL
     REYEANGQGF QRLALLEEEK ALPWNAVWDM FCLKNNVPVG EDFIAEIEKY EAEVTSKR
//