ID   RHAAB_ALKCK             Reviewed;         894 AA.
AC   Q5WL39;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Bifunctional enzyme RhaA/RhaB;
DE   Includes:
DE     RecName: Full=Rhamnulokinase;
DE              EC=2.7.1.5;
DE     AltName: Full=Rhamnulose kinase;
DE   Includes:
DE     RecName: Full=L-rhamnose isomerase;
DE              EC=5.3.1.14;
GN   Name=rhaAB; OrderedLocusNames=ABC0374;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-rhamnulose = ADP + H(+) + L-rhamnulose 1-phosphate;
CC         Xref=Rhea:RHEA:20117, ChEBI:CHEBI:15378, ChEBI:CHEBI:17897,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58313, ChEBI:CHEBI:456216; EC=2.7.1.5;
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation; glycerone
CC       phosphate from L-rhamnose: step 1/3.
CC   -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation; glycerone
CC       phosphate from L-rhamnose: step 2/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the rhamnulokinase
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the rhamnose
CC       isomerase family. {ECO:0000305}.
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DR   EMBL; AP006627; BAD62916.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5WL39; -.
DR   SMR; Q5WL39; -.
DR   STRING; 66692.ABC0374; -.
DR   EnsemblBacteria; BAD62916; BAD62916; ABC0374.
DR   KEGG; bcl:ABC0374; -.
DR   eggNOG; COG1070; Bacteria.
DR   eggNOG; COG4806; Bacteria.
DR   HOGENOM; CLU_323306_0_0_9; -.
DR   UniPathway; UPA00541; UER00601.
DR   UniPathway; UPA00541; UER00602.
DR   Proteomes; UP000001168; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0008993; F:rhamnulokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019301; P:rhamnose catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07771; FGGY_RhuK; 1.
DR   HAMAP; MF_00541; RhaA; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018485; Carb_kinase_FGGY_C.
DR   InterPro; IPR018484; Carb_kinase_FGGY_N.
DR   InterPro; IPR009308; Rhamnose_isomerase.
DR   InterPro; IPR013449; Rhamnulokinase.
DR   InterPro; IPR036237; Xyl_isomerase-like_sf.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   Pfam; PF06134; RhaA; 1.
DR   SUPFAM; SSF51658; SSF51658; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR01748; rhaA; 1.
DR   TIGRFAMs; TIGR02627; rhamnulo_kin; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Isomerase; Kinase; Manganese; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding; Reference proteome;
KW   Rhamnose metabolism; Transferase.
FT   CHAIN           1..894
FT                   /note="Bifunctional enzyme RhaA/RhaB"
FT                   /id="PRO_0000090570"
FT   REGION          1..465
FT                   /note="Rhamnulokinase"
FT   REGION          466..894
FT                   /note="L-rhamnose isomerase"
FT   BINDING         730
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         762
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         764
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   894 AA;  100288 MW;  67FF1781A46CAAAA CRC64;
     MGEYRLAVDI GASSGRVMAG KISEAGIDLQ EVYRFDNQAQ LMGGHYCWDV DHLFGEIKKG
     IRVAVQSGLQ PVSIGMNTWA VDFVLLDEKG ERLTDAISYR DPRTNGVMEG VIETYGKKAL
     YERTGIAFQP FNTLYQLLAL KKQNPELLEQ AHAFLMVPDY FHFLLTGVKV NEYTNATTTQ
     LVNVHTKDWD RQLLKEFGLP CGMFQPLQHP GTKIGSLTES MEKELGVQLE VIVPATHDTA
     SAIAALPEKQ TSVYISSGTW SLIGIENRTP ICSQQAMAAN FTNEGGVGSR IRFLKNIMGL
     WMIQEVQRLL PGHWSFSQLA QAASESTYTG EIDVDQHRFL KPENMIEEIQ QACREKGLAV
     PESPGDLAKC IYDSLIASYD KAVTEIEAIS GKPYEQIHII GGGALNKEIN QRLANRTNKT
     VIAGPTEATA VGNLLVQAIA DGELSRIEEG RALVRTAFPV TYFLPQRSES HVSSRFESAK
     VQYEQLGIDV EAAFAKVKQV PISVHCWQGD DLHGTEVIAN ELSGGIDVTG NHPGRARNGE
     ELRRDLEKAL SLIPGKHRVN LHAMYAETDS VPIERDQLKT EHFEKWVKWA KSLGIGLDFN
     PTVFSHPKAA DGLTLAHPDE EIRTFWINHC KACRKIAAYF GEQLGTPSLV NIWVPDGYKD
     TPSDRLTPRK RLKESLDAIY ADEYDPMLVL DTVESKLFGI GSEAYVVGSH EFYLNYANQN
     NKLYLLDTGH FHPTEVVSNK LSAMLLFHDQ LALHVSRPVR WDSDHVVTFD DELREIAIEL
     VRNDALGNIH IGLDFFDASI NRVAAWAIGT RNMAKALLYA ALMPHRHLKQ LQDEGDFTSR
     LAMQEQLKTY PFGDMWDEYC KRQGVPTETE WLDVVKEYEQ QVQLKRESEK AKQR