ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry B1IVH4


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name RHAB_ECOLC
Primary accession number B1IVH4
Secondary accession numbers None
Integrated into Swiss-Prot on May 20, 2008
Sequence was last modified on April 29, 2008 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 7)
Name and origin of the protein
Protein name Rhamnulokinase
Synonyms EC 2.7.1.5
Rhamnulose kinase
Gene name
Name: rhaB
OrderedLocusNames: EcolC_4113
From
Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks) [TaxID: 481805] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Ingram L., Richardson P.;
"Complete sequence of Escherichia coli C str. ATCC 8739.";
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CP000946; ACA79711.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001727038.1; -.
3D structure databases
ModBase B1IVH4.
Ontologies
GO
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008993; Molecular function: rhamnulokinase activity (inferred from electronic annotation from HAMAP).
GO:0019301; Biological process: rhamnose catabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
HAMAP MF_01535; -; 1.
PBIL [Tree]
InterPro IPR000577; FGGY_kin.
IPR013449; Rhamnulokinase.
Graphical view of domain structure.
PANTHER PTHR10196; FGGY_kin; 1.
Pfam PF00370; FGGY_N; 1.
Pfam graphical view of domain structure.
Genome annotation databases
GeneID 6065939; -.
GenomeReviews CP000946_GR; EcolC_4113.
KEGG ecl:EcolC_4113; -.
CMR B1IVH4; EcolC_4113.
Other
ProtoNet B1IVH4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Complete proteome; Kinase; Nucleotide-binding; Rhamnose metabolism; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   489  489     Rhamnulokinase. PRO_1000087601
REGION   236   238  3     Substrate binding (By similarity). 
BINDING   14    14        ATP (By similarity). 
BINDING   259   259        ATP (By similarity). 
BINDING   296   296        Substrate (By similarity). 
BINDING   304   304        ATP (By similarity). 
Sequence information
Length: 489 AA [This is the length of the unprocessed precursor] Molecular weight: 54069 Da [This is the MW of the unprocessed precursor] CRC64: AF66259EACAC5F4E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTFRNCVAVD LGASSGRVML ARYERECRSL TLREIHRFNN GLHSQNGYVT WDVDSLESAI 

        70         80         90        100        110        120 
RLGLNKVCEE GIRIDSIGID TWGVDFVLLD QQGQRVGLPV AYRDSRTNGL MAQAQQQLGK 

       130        140        150        160        170        180 
RDIYQRSGIQ FLPFNTLYQL RALTEQQPEL IPHIAHALLM PDYFSYRLTG KMNWEYTNAT 

       190        200        210        220        230        240 
TTQLVNINSD DWDESLLAWS GANKAWFGRP THPGNVIGHW ICPQGNEIPV VAVASHDTAS 

       250        260        270        280        290        300 
AVIASPLNGS RAAYLSSGTW SLMGFESQTP FTNDTALAAN ITNEGGAEGR YRVLKNIMGL 

       310        320        330        340        350        360 
WLLQRVLQEQ QINDLPALIS ATQALPACRF IINPNDDRFI NPETMCSEIQ AACRETAQPI 

       370        380        390        400        410        420 
PESDAELARC IFDSLALLYA DVLHELAQLR GEDFSQLHIV GGGCQNTLLN QLCADACGIR 

       430        440        450        460        470        480 
VIAGPVEAST LGNIGIQLMT LDELNNVDDF RQVVSTTANL TTFTPNPDSE IAHYVAQIHS 


TRQTKELCA 

B1IVH4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!