ID   RHAB_SHISS              Reviewed;         489 AA.
AC   Q3YV72;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Rhamnulokinase;
DE            EC=2.7.1.5;
DE   AltName: Full=Rhamnulose kinase;
GN   Name=rhaB; OrderedLocusNames=SSON_4074;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ90590.1; -; Genomic_DNA.
DR   RefSeq; YP_312825.1; -.
DR   SMR; Q3YV72; 2-480.
DR   GeneID; 3669301; -.
DR   GenomeReviews; CP000038_GR; SSON_4074.
DR   KEGG; ssn:SSON_4074; -.
DR   HOGENOM; Q3YV72; -.
DR   OMA; Q3YV72; EIHRFKN.
DR   BioCyc; SSON300269:SSO_4074-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;
KW   Rhamnose metabolism; Transferase.
FT   CHAIN         1    489       Rhamnulokinase.
FT                                /FTId=PRO_0000297524.
FT   REGION      236    238       Substrate binding (By similarity).
FT   BINDING      14     14       ATP (By similarity).
FT   BINDING     259    259       ATP (By similarity).
FT   BINDING     296    296       Substrate (By similarity).
FT   BINDING     304    304       ATP (By similarity).
SQ   SEQUENCE   489 AA;  54066 MW;  DE40F471DC7BD50B CRC64;
     MTFRNCVAVD LGASSGRVML ARYERECRSL TLREIHRFNN GLHSQNGYVT WNVDSLESAI
     RLGLNKVCEE GIRIDSIGID TWGVDFVLLD QQGQRVGLPV AYRDSRSNGL MAQAQQQLGK
     RDIYQRSGIQ FLPFNTLYQL RALTEQQPEL IPHIAHALLM PDYFSYRLTG KMNWEYTNAT
     TTQLVNINSD DWDESLLAWS GANKAWFGRP THPGNVIGHW ICPQGNEIPV VAVASHDTAS
     AVIASPLNGS RAAYLSSGTW SLMGFESQTP FTNDTALAAN ITNEGGAEGR YRVLKNIMGL
     WLLQRVLQER QINDLPALIA ATQALPACRF IINPNDDRFI NPEAMCSEIQ AACREMAQPL
     PESDAELARC IFDSLALLYA DVLHELAQLR GEDFSQLHIV GGGCQNTLLN QLCADACGIR
     VIAGPVEAST LGNIGIQLMT LDELNNVDDF RQVVSTTANL TTFTPNPDSE IAHYVAQLHS
     TRQTKELCA
//