ID RHAAB_BACSK Reviewed; 894 AA.
AC Q5WL39;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 02-NOV-2016, entry version 77.
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 Bacillus clausii (strain KSM-K16).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
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
RT KSM-K16.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY: ATP + L-rhamnulose = ADP + L-rhamnulose 1-
CC phosphate.
CC -!- CATALYTIC ACTIVITY: L-rhamnopyranose = L-rhamnulose.
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;
CC glycerone phosphate from L-rhamnose: step 1/3.
CC -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation;
CC glycerone phosphate from L-rhamnose: step 2/3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC rhamnulokinase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the rhamnose
CC isomerase family. {ECO:0000305}.
DR EMBL; AP006627; BAD62916.1; -; Genomic_DNA.
DR ProteinModelPortal; Q5WL39; -.
DR SMR; Q5WL39; -.
DR STRING; 66692.ABC0374; -.
DR EnsemblBacteria; BAD62916; BAD62916; ABC0374.
DR KEGG; bcl:ABC0374; -.
DR PATRIC; 18919968; VBIBacCla58185_0389.
DR eggNOG; ENOG4105DKG; Bacteria.
DR eggNOG; COG1070; LUCA.
DR eggNOG; COG4806; LUCA.
DR KO; K00848; -.
DR KO; K01813; -.
DR OrthoDB; POG091H0HAV; -.
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-EC.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0008993; F:rhamnulokinase activity; IEA:UniProtKB-EC.
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; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR InterPro; IPR009308; Rhamnose_isomerase.
DR InterPro; IPR013449; Rhamnulokinase.
DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR Pfam; PF06134; RhaA; 1.
DR SUPFAM; SSF51658; SSF51658; 1.
DR TIGRFAMs; TIGR01748; rhaA; 1.
DR TIGRFAMs; TIGR02627; rhamnulo_kin; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Cytoplasm; Isomerase; Kinase;
KW Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW Reference proteome; Rhamnose metabolism; Transferase.
FT CHAIN 1 894 Bifunctional enzyme RhaA/RhaB.
FT /FTId=PRO_0000090570.
FT REGION 1 465 Rhamnulokinase.
FT REGION 466 894 L-rhamnose isomerase.
FT METAL 730 730 Manganese. {ECO:0000250}.
FT METAL 762 762 Manganese. {ECO:0000250}.
FT METAL 764 764 Manganese. {ECO:0000250}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 462 894 ihamap:RhaA [T]
FT MYHIT 4 242 ipfam:FGGY_N [T]
FT MYHIT 254 440 ipfam:FGGY_C [T]
FT MYHIT 472 886 ipfam:RhaA [T]
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
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