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UniProtKB/Swiss-Prot entry P32171


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

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Entry information
Entry name RHAB_ECOLI
Primary accession number P32171
Secondary accession number Q2M8K1
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on October 1, 1993 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 63)
Name and origin of the protein
Protein name Rhamnulokinase
Synonyms EC 2.7.1.5
Rhamnulose kinase
Gene name
Name: rhaB
OrderedLocusNames: b3904, JW3875
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=8396120 [NCBI, ExPASy, EBI, Israel, Japan]
Moralejo P., Egan S.M., Hidalgo E.F., Aguilar J.;
"Sequencing and characterization of a gene cluster encoding the enzymes for L-rhamnose metabolism in Escherichia coli.";
J. Bacteriol. 175:5585-5594(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1093/nar/21.15.3391; PubMed=8346018 [NCBI, ExPASy, EBI, Israel, Japan]
Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes.";
Nucleic Acids Res. 21:3391-3398(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
INDUCTION.
STRAIN=ECL116;
DOI=10.1006/jmbi.1993.1565; PubMed=8230210 [NCBI, ExPASy, EBI, Israel, Japan]
Egan S.M., Schleif R.F.;
"A regulatory cascade in the induction of rhaBAD.";
J. Mol. Biol. 234:87-98(1993).
[6]
INDUCTION.
DOI=10.1128/JB.182.12.3529-3535.2000; PubMed=10852886 [NCBI, ExPASy, EBI, Israel, Japan]
Holcroft C.C., Egan S.M.;
"Roles of cyclic AMP receptor protein and the carboxyl-terminal domain of the alpha subunit in transcription activation of the Escherichia coli rhaBAD operon.";
J. Bacteriol. 182:3529-3535(2000).
[7]
X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) IN COMPLEX WITH ADP AND FRUCTOSE, AND SUBUNIT.
DOI=10.1016/j.jmb.2006.04.013; PubMed=16674975 [NCBI, ExPASy, EBI, Israel, Japan]
Grueninger D., Schulz G.E.;
"Structure and reaction mechanism of L-rhamnulose kinase from Escherichia coli.";
J. Mol. Biol. 359:787-797(2006).
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
X60472; CAA43001.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L19201; AAB03037.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76886.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77405.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S40848; S40848.
RefSeq AP_003904.1; -.
NP_418340.1; -.
3D structure databases
PDB
2CGJ; X-ray; 2.26 A; A=1-489.[ExPASy / RCSB / EBI]
2CGK; X-ray; 2.46 A; A/B=1-489.[ExPASy / RCSB / EBI]
2CGL; X-ray; 1.88 A; A=1-489.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2CGJ; -.
2CGK; -.
2CGL; -.
SMR P32171; 2-480.
ModBase P32171.
Enzyme and pathway databases
BioCyc EcoCyc:RHAMNULOKIN-MON; -.
MetaCyc:RHAMNULOKIN-MON; -.
Organism-specific databases
EchoBASE EB1814; -.
EcoGene EG11868; rhaB.
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.
TIGRFAMs TIGR02627; rhamnulo_kin; 1.
BLOCKS P32171.
ProtoNet P32171.
Genome annotation databases
GeneID 948399; -.
GenomeReviews U00096_GR; b3904.
AP009048_GR; JW3875.
KEGG ecj:JW3875; -.
eco:b3904; -.
Phylogenomic databases
HOGENOM P32171; -.
Genome annotation databases
CMR P32171; b3904.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; 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_0000090531
REGION   236   238  3     Substrate binding. 
BINDING   14    14        ATP. 
BINDING   259   259        ATP. 
BINDING   296   296        Substrate. 
BINDING   304   304        ATP. 
CONFLICT   214   214        Missing (in Ref. 1; CAA43001). 
CONFLICT   388   389        QL -> HV (in Ref. 1; CAA43001). 
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 

P32171 in FASTA format

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View entry in raw text format (no links)
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