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P32171 (RHAB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rhamnulokinase

EC=2.7.1.5
Alternative name(s):
Rhamnulose kinase
Gene names
Name:rhaB
Ordered Locus Names:b3904, JW3875
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length489 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + L-rhamnulose = ADP + L-rhamnulose 1-phosphate. HAMAP MF_01535

Pathway

Carbohydrate degradation; L-rhamnose degradation; glycerone phosphate from L-rhamnose: step 2/3. HAMAP MF_01535

Subunit structure

Monomer. Ref.7

Induction

Induced by L-rhamnose via the rhaR-rhaS regulatory cascade. Binding of the cAMP receptor protein (CRP) is required for full expression. Ref.5 Ref.6

Sequence similarities

Belongs to the rhamnulokinase family.

Sequence caution

The sequence CAA43001.1 differs from that shown. Reason: Frameshift at position 398.

Ontologies

Keywords
   Biological processRhamnose metabolism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processrhamnose catabolic process

Inferred from mutant phenotype. Source: EcoCyc

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

rhamnulokinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 489489Rhamnulokinase HAMAP MF_01535
PRO_0000090531

Regions

Region236 – 2383Substrate binding HAMAP MF_01535

Sites

Binding site141ATP
Binding site2591ATP
Binding site2961Substrate
Binding site3041ATP

Experimental info

Sequence conflict2141Missing in CAA43001. Ref.1
Sequence conflict388 – 3892QL → HV in CAA43001. Ref.1

Secondary structure

................................................................................ 489
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32171 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: AF66259EACAC5F4E

FASTA48954,069
        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 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing and characterization of a gene cluster encoding the enzymes for L-rhamnose metabolism in Escherichia coli."
Moralejo P., Egan S.M., Hidalgo E.F., Aguilar J.
J. Bacteriol. 175:5585-5594(1993) [PubMed: 8396120] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 21:3391-3398(1993) [PubMed: 8346018] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"A regulatory cascade in the induction of rhaBAD."
Egan S.M., Schleif R.F.
J. Mol. Biol. 234:87-98(1993) [PubMed: 8230210] [Abstract]
Cited for: INDUCTION.
Strain: ECL116.
[6]"Roles of cyclic AMP receptor protein and the carboxyl-terminal domain of the alpha subunit in transcription activation of the Escherichia coli rhaBAD operon."
Holcroft C.C., Egan S.M.
J. Bacteriol. 182:3529-3535(2000) [PubMed: 10852886] [Abstract]
Cited for: INDUCTION.
[7]"Structure and reaction mechanism of L-rhamnulose kinase from Escherichia coli."
Grueninger D., Schulz G.E.
J. Mol. Biol. 359:787-797(2006) [PubMed: 16674975] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) IN COMPLEX WITH ADP AND FRUCTOSE, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60472 Genomic DNA. Translation: CAA43001.1. Frameshift.
L19201 Genomic DNA. Translation: AAB03037.1.
U00096 Genomic DNA. Translation: AAC76886.1.
AP009048 Genomic DNA. Translation: BAE77405.1.
PIRS40848.
RefSeqNP_418340.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CGJX-ray2.26A1-489[»]
2CGKX-ray2.46A/B1-489[»]
2CGLX-ray1.88A1-489[»]
ProteinModelPortalP32171.
SMRP32171. Positions 2-480.
ModBaseSearch...

Protein-protein interaction databases

IntActP32171. 2 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000000399; EBESCP00000000399; EBESCG00000000329.
EBESCT00000014805; EBESCP00000014096; EBESCG00000013865.
GeneID948399.
GenomeReviewsGene locus JW3875 in contig AP009048_GR.
Gene locus b3904 in contig U00096_GR.
KEGGecj:JW3875.
eco:b3904.
PATRIC32123317. VBIEscCol129921_4019.

Organism-specific databases

EchoBASEEB1814.
EcoGeneEG11868. rhaB.

Phylogenomic databases

eggNOGCOG1070.
GeneTreeEBGT00050000009230.
HOGENOMHBG313195.
OMAKENYTNE.
PhylomeDBP32171.
ProtClustDBPRK10640.

Enzyme and pathway databases

BioCycEcoCyc:RHAMNULOKIN-MONOMER.
MetaCyc:RHAMNULOKIN-MONOMER.

Gene expression databases

GenevestigatorP32171.

Family and domain databases

HAMAPMF_01535. Rhamnulokinase.
[Tree]
InterProIPR000577. Carb_kinase_FGGY.
IPR018485. Carb_kinase_FGGY_C.
IPR018484. Carb_kinase_FGGY_N.
IPR013449. Rhamnulokinase.
[Graphical view]
KOK00848.
PANTHERPTHR10196. FGGY_kin. 1 hit.
PfamPF02782. FGGY_C. 1 hit.
PF00370. FGGY_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR02627. Rhamnulo_kin. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRHAB_ECOLI
AccessionPrimary (citable) accession number: P32171
Secondary accession number(s): Q2M8K1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: January 25, 2012
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families