ID   RHAB_LACS1              Reviewed;         485 AA.
AC   Q1WRE4;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Rhamnulokinase;
DE            EC=2.7.1.5;
DE   AltName: Full=Rhamnulose kinase;
GN   Name=rhaB; OrderedLocusNames=LSL_1752;
OS   Lactobacillus salivarius subsp. salivarius (strain UCC118).
OG   Plasmid pMP118.
OC   Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=362948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA   Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA   Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C.,
RA   Collins J.K., Higgins D., Shanahan F., Fitzgerald G.F.,
RA   van Sinderen D., O'Toole P.W.;
RT   "Multireplicon genome architecture of Lactobacillus salivarius.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
CC   -!- CATALYTIC ACTIVITY: ATP + L-rhamnulose = ADP + L-rhamnulose 1-
CC       phosphate.
CC   -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation;
CC       glycerone phosphate from L-rhamnose: step 2/3.
CC   -!- SIMILARITY: Belongs to the rhamnulokinase family.
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DR   EMBL; CP000234; ABE00554.1; -; Genomic_DNA.
DR   RefSeq; YP_536637.1; -.
DR   GeneID; 3978502; -.
DR   GenomeReviews; CP000234_GR; LSL_1752.
DR   KEGG; lsl:LSL_1752; -.
DR   HOGENOM; Q1WRE4; -.
DR   OMA; Q1WRE4; EIHRFKN.
DR   BioCyc; LSAL362948:LSL_1752-MON; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008993; F:rhamnulokinase activity; IEA:HAMAP.
DR   GO; GO:0019301; P:rhamnose catabolic process; IEA:InterPro.
DR   HAMAP; MF_01535; -; 1.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018484; Carb_kinase_FGGY_N.
DR   InterPro; IPR013449; Rhamnulokinase.
DR   PANTHER; PTHR10196; FGGY_kin; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   TIGRFAMs; TIGR02627; rhamnulo_kin; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Kinase; Nucleotide-binding; Plasmid;
KW   Rhamnose metabolism; Transferase.
FT   CHAIN         1    485       Rhamnulokinase.
FT                                /FTId=PRO_0000292778.
FT   REGION      234    236       Substrate binding (By similarity).
FT   BINDING      12     12       ATP (By similarity).
FT   BINDING     257    257       ATP (By similarity).
FT   BINDING     294    294       Substrate (By similarity).
FT   BINDING     302    302       ATP (By similarity).
SQ   SEQUENCE   485 AA;  54821 MW;  ABD197EA0C062364 CRC64;
     MKAYVAVDIG ASSGRLMLGQ LEDGKLKLQE MHRFKNGFEF KNNHDRWNID YLIDEIFKGL
     EKIKESGYTE VSLGIDTWAV DYVLVGKDGK KLQDPISYRD KRTSNSINEL TTEVSKEYIY
     KKTGIQFLNF NTLYQLFEED KELLKKTDKI MMIPDYIGYI LTGKAVTEIT NASTTQMLSL
     REGLFDKNLL EKVNVSSDQF AKLVDAGTVL GNLKEDWYSK YELPKVNVVT VATHDTASAV
     IGTPCEGQHW AYLSSGTWSL IGTELNIPEN GAKVFKENYT NEWGAYGTYR FLKNIMGLWM
     AQCVKKELND QYSFSELAEL AGEVEPFEQF INVNDQRFQN PGNMIQEIQT YCRETGQKVP
     ETPGEIMMAI YSNLALFYAN EISKLDDIMG YHIDTLNIVG GGSNVALMNQ LTSTIANVDV
     YAGPSEATAI GNILVQMITA GDVLNVYLGR RIISNSFDIK HYTPEQGKYS KVLAEYQQFL
     NKERG
//