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Reviewed, UniProtKB/Swiss-Prot Q1R415 (RHAB_ECOUT)

Last modified June 16, 2009. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Rhamnulokinase
    EC=2.7.1.5
Alternative name(s):
    Rhamnulose kinase
Gene names
Name: rhaB
Ordered Locus Names: UTI89_C4487
OrganismEscherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier364106 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length489 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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 By similarity.

Sequence similarities

Belongs to the rhamnulokinase family.

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Ontologies

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

Inferred from electronic annotation. Source: InterPro

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

rhamnulokinase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 489489Rhamnulokinase HAMAP MF_01535
PRO_0000297519

Regions

Region236 – 2383Substrate binding By similarity

Sites

Binding site141ATP By similarity
Binding site2591ATP By similarity
Binding site2961Substrate By similarity
Binding site3041ATP By similarity

Secondary structure

1 ....................................................................................... 489
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q1R415-1 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: E2B573E7AE58CA24

FASTA48954,076
        10         20         30         40         50         60 
MTFRNCVAVD LGASSGRVML ARYERECRSL TLREIHRFNN GLHSQNGYVT WNVDSLESAI 

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

       130        140        150        160        170        180 
RDIYQRSGIQ FLPFNTIYQL RALTEQQPEL IPHIAHALLI 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 
WLLQRVLQER QINDLPALIA ATQALPACRF IINPNDDRFI NPDEMCSEIQ 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

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References

[1]"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach."
Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed: 16585510] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

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Cross-references

Sequence databases

CP000243 Genomic DNA. Translation: ABE09899.1.
RefSeqYP_543430.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2UYTX-ray1.55A1-489[»]
SMRQ1R415. Positions 2-480.
ModBaseSearch...

Genome annotation databases

GeneID3992418.
GenomeReviewsGene locus UTI89_C4487 in contig CP000243_GR.
KEGGeci:UTI89_C4487.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1R415.
OMAQ1R415. EIHRFKN.

Enzyme and pathway databases

BioCycECOL364106:UTI89_C4487-MON.

Family and domain databases

HAMAPMF_01535.
[Tree]
InterProIPR000577. Carb_kinase_FGGY.
IPR018484. Carb_kinase_FGGY_N.
IPR013449. Rhamnulokinase.
[Graphical view]
PANTHERPTHR10196. FGGY_kin. 1 hit.
PfamPF00370. FGGY_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR02627. rhamnulo_kin. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameRHAB_ECOUT
AccessionPrimary (citable) accession number: Q1R415
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: May 16, 2006
Last modified: June 16, 2009
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents