ID RHAB_ECOLC Reviewed; 489 AA. AC B1IVH4; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 16-JUN-2009, entry version 10. DE RecName: Full=Rhamnulokinase; DE EC=2.7.1.5; DE AltName: Full=Rhamnulose kinase; GN Name=rhaB; OrderedLocusNames=EcolC_4113; OS Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=481805; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Ingram L., Richardson P.; RT "Complete sequence of Escherichia coli C str. ATCC 8739."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000946; ACA79711.1; -; Genomic_DNA. DR RefSeq; YP_001727038.1; -. DR GeneID; 6065939; -. DR GenomeReviews; CP000946_GR; EcolC_4113. DR KEGG; ecl:EcolC_4113; -. DR OMA; B1IVH4; EIHRFKN. 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_1000087601. 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; 54069 MW; AF66259EACAC5F4E CRC64; MTFRNCVAVD LGASSGRVML ARYERECRSL TLREIHRFNN GLHSQNGYVT WDVDSLESAI RLGLNKVCEE GIRIDSIGID TWGVDFVLLD QQGQRVGLPV AYRDSRTNGL MAQAQQQLGK RDIYQRSGIQ FLPFNTLYQL RALTEQQPEL IPHIAHALLM PDYFSYRLTG KMNWEYTNAT TTQLVNINSD DWDESLLAWS GANKAWFGRP THPGNVIGHW ICPQGNEIPV VAVASHDTAS AVIASPLNGS RAAYLSSGTW SLMGFESQTP FTNDTALAAN ITNEGGAEGR YRVLKNIMGL WLLQRVLQEQ QINDLPALIS ATQALPACRF IINPNDDRFI NPETMCSEIQ AACRETAQPI PESDAELARC IFDSLALLYA DVLHELAQLR GEDFSQLHIV GGGCQNTLLN QLCADACGIR VIAGPVEAST LGNIGIQLMT LDELNNVDDF RQVVSTTANL TTFTPNPDSE IAHYVAQIHS TRQTKELCA //