RHAA_BACTN
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 03-AUG-2022, entry version 104.
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=BT_3764;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
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 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(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; AE015928; AAO78869.1; -; Genomic_DNA.
DR RefSeq; NP_812675.1; NC_004663.1.
DR RefSeq; WP_010536410.1; NC_004663.1.
DR AlphaFoldDB; Q8A1A2; -.
DR SMR; Q8A1A2; -.
DR STRING; 226186.BT_3764; -.
DR PaxDb; Q8A1A2; -.
DR PRIDE; Q8A1A2; -.
DR EnsemblBacteria; AAO78869; AAO78869; BT_3764.
DR GeneID; 45363319; -.
DR GeneID; 60924934; -.
DR KEGG; bth:BT_3764; -.
DR PATRIC; fig|226186.12.peg.3826; -.
DR eggNOG; COG4806; Bacteria.
DR HOGENOM; CLU_052790_0_0_10; -.
DR InParanoid; Q8A1A2; -.
DR OMA; HKVNLHA; -.
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; 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.
PE 3: Inferred from homology;
KW Cytoplasm; Isomerase; Manganese; Metal-binding; Reference proteome;
KW Rhamnose metabolism.
FT CHAIN 1..418
FT /note="L-rhamnose isomerase"
FT /id="PRO_0000090551"
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 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