ID   RHAB_ECOL5              Reviewed;         489 AA.
AC   Q0TAF9;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Rhamnulokinase;
DE            EC=2.7.1.5;
DE   AltName: Full=Rhamnulose kinase;
GN   Name=rhaB; OrderedLocusNames=ECP_4114;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(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   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: Belongs to the rhamnulokinase family.
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DR   EMBL; CP000247; ABG72070.1; -; Genomic_DNA.
DR   RefSeq; YP_671971.1; -.
DR   SMR; Q0TAF9; 2-480.
DR   GeneID; 4189734; -.
DR   GenomeReviews; CP000247_GR; ECP_4114.
DR   KEGG; ecp:ECP_4114; -.
DR   NMPDR; fig|340197.3.peg.2774; -.
DR   HOGENOM; Q0TAF9; -.
DR   OMA; Q0TAF9; EIHRFKN.
DR   BioCyc; ECOL362663:ECP_4114-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_0000297521.
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;  54115 MW;  02F0D88AC4AC8F7A CRC64;
     MTFRNCVAVD LGASSGRVML ARYERECRSL TLREIHRFNN GLHSQNGYVT WNVDRLESAI
     RLGLNKVCEE GIRIDSIGID TWGVDFVLLD QQGQRVGLPV AYRDSRTNGL MAQAQQQLGK
     RDIYQRSGIQ FLPFNTIYQL RALTEQQPEL IPHIAHALLI PDYFSYRLTG KMNWEYTNAT
     TTQLVNINSD DWDESLLAWS GANKAWFGRP THPGNVIGHW ICPQGNEIPV VAVASHDTAS
     AVIASPLNGS RAAYLSSGTW SLMGFESQTP FTNDTALAAN ITNEGGAEGR YRVLKNIMGL
     WLLQRVLQER QINDLPALIA ATQALPACRF IINPNDDRFI NPDEMCSEIQ AACRETAQPI
     PESDAELARC IFDSLALLYA DVLHELAQLR GEDFSQLHIV GGGCQNALLN QLCADACGIR
     VIAGPVEAST LGNIGIQLMT LDELNNVDDF RQVVSTTANL TTFTPNPDSE IAHYVAQIHS
     TRQTKELCA
//