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RHAA_CLOB8
ID   RHAA_CLOB8              Reviewed;         418 AA.
AC   A6LQK4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Cbei_0446;
OS   Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS   acetobutylicum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=290402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA   Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA   Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA   Blaschek H., Richardson P.;
RT   "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000721; ABR32634.1; -; Genomic_DNA.
DR   RefSeq; WP_011967795.1; NC_009617.1.
DR   AlphaFoldDB; A6LQK4; -.
DR   SMR; A6LQK4; -.
DR   STRING; 290402.Cbei_0446; -.
DR   EnsemblBacteria; ABR32634; ABR32634; Cbei_0446.
DR   KEGG; cbe:Cbei_0446; -.
DR   eggNOG; COG4806; Bacteria.
DR   HOGENOM; CLU_052790_0_0_9; -.
DR   OMA; HKVNLHA; -.
DR   OrthoDB; 283831at2; -.
DR   UniPathway; UPA00541; UER00601.
DR   Proteomes; UP000000565; 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..418
FT                   /note="L-rhamnose isomerase"
FT                   /id="PRO_1000081935"
FT   BINDING         261
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00541"
FT   BINDING         293
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00541"
FT   BINDING         295
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00541"
SQ   SEQUENCE   418 AA;  48128 MW;  560ED6C61A7DEF9E CRC64;
     MNVKEKYELA KKEYEKWGID VDKVLDELNK VKISIHCWQG DDVKGFEVVQ NELSGGIQCN
     GNYPGAARNA EELRKDLDKA LSLIPGKHKV NLHAIYLETN GEFVDRDEIK PEHFANWVKW
     AKENGLGLDF NPTIFSHPKS ADGLTLSHPD KEIRDFWIRH SIASRKIGEY FGKELGQTCL
     TNIWIPDGYK DIPSDRLGPR RRLKESLDEI FKVQIDKKYN LDCVESKVFG IGAEAYTVGS
     NEFYLNYAAK NNIMSLMDTG HYHPTEVVSD KLSAMLLFDE KVALHVSRPV RWDSDHVVVY
     DDELKEIAKE IVRNDALDRV IIGLDFFDAS INRIAAWTIG SRNMIKALLN AMLTPNDKLR
     ELQEEGNFTE RLALMEEFKT YPMGDIWNYY CEKNNVPVGE SWIKEVKEYE KDVLSKRN
 
 
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