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Reviewed, UniProtKB/Swiss-Prot P08204 (ARAB_ECOLI)

Last modified February 9, 2010. Version 87. 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 · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Ribulokinase
    EC=2.7.1.16
Gene names
Name: araB
Ordered Locus Names: b0063, JW0062
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length566 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

ATP + L(or D)-ribulose = ADP + L(or D)-ribulose 5-phosphate. HAMAP MF_00520

Pathway

Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 2/3. HAMAP MF_00520

Sequence similarities

Belongs to the ribulokinase family.

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Ontologies

Keywords
   Biological processArabinose catabolism
Carbohydrate metabolism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processL-arabinose catabolic process to xylulose 5-phosphate

Inferred from expression pattern. Source: UniProtKB

   Cellular componentcytoplasm

Inferred from direct assay. Source: UniProtKB

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction. Source: IntAct

ribulokinase activity

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

nadEP188431EBI-1113458,EBI-548960

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 566565Ribulokinase HAMAP MF_00520
PRO_0000198358

Experimental info

Sequence conflict231T → S Ref.1
Sequence conflict231T → S Ref.2
Sequence conflict127 – 1282EA → RS Ref.1
Sequence conflict127 – 1282EA → RS Ref.2
Sequence conflict3501G → S Ref.1
Sequence conflict3501G → S Ref.2
Sequence conflict3651T → A Ref.1
Sequence conflict3651T → A Ref.2
Sequence conflict4031T → S Ref.1
Sequence conflict4031T → S Ref.2
Sequence conflict5251C → R Ref.1
Sequence conflict5251C → R Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P08204-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 4A12010092139D8A

FASTA56661,089
        10         20         30         40         50         60 
MAIAIGLDFG SDSVRALAVD CATGEEIATS VEWYPRWQKG QFCDAPNNQF RHHPRDYIES 

        70         80         90        100        110        120 
MEAALKTVLA ELSVEQRAAV VGIGVDSTGS TPAPIDADGN VLALRPEFAE NPNAMFVLWK 

       130        140        150        160        170        180 
DHTAVEEAEE ITRLCHAPGN VDYSRYIGGI YSSEWFWAKI LHVTRQDSAV AQSAASWIEL 

       190        200        210        220        230        240 
CDWVPALLSG TTRPQDIRRG RCSAGHKSLW HESWGGLPPA SFFDELDPIL NRHLPSPLFT 

       250        260        270        280        290        300 
DTWTADIPVG TLCPEWAQRL GLPESVVISG GAFDCHMGAV GAGAQPNALV KVIGTSTCDI 

       310        320        330        340        350        360 
LIADKQSVGE RAVKGICGQV DGSVVPGFIG LEAGQSAFGD IYAWFGRVLG WPLEQLAAQH 

       370        380        390        400        410        420 
PELKTQINAS QKQLLPALTE AWAKNPSLDH LPVVLDWFNG RRTPNANQRL KGVITDLNLA 

       430        440        450        460        470        480 
TDAPLLFGGL IAATAFGARA IMECFTDQGI AVNNVMALGG IARKNQVIMQ ACCDVLNRPL 

       490        500        510        520        530        540 
QIVASDQCCA LGAAIFAAVA AKVHADIPSA QQKMASAVEK TLQPCSEQAQ RFEQLYRRYQ 

       550        560 
QWAMSAEQHY LPTSAPAQAA QAVATL

« Hide

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References

« Hide 'large scale' references
[1]"The organization of the araBAD operon of Escherichia coli."
Lee N., Gielow W., Martin R., Hamilton E., Fowler A.
Gene 47:231-244(1986) [PubMed: 3549454] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
Nucleic Acids Res. 20:3305-3308(1992) [PubMed: 1630901] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12.
[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], SEQUENCE REVISION.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Nucleotide sequence of the 5' end of araBAD operon messenger RNA in Escherichia coli B/r."
Lee N., Carbon J.
Proc. Natl. Acad. Sci. U.S.A. 74:49-53(1977) [PubMed: 189315] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-14, PROTEIN SEQUENCE OF 2-14.
[6]"Nucleotide sequence of the L-arabinose regulatory region of Escherichia coli K12."
Smith B.R., Schleif R.
J. Biol. Chem. 253:6931-6933(1978) [PubMed: 357433] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
Strain: K12.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M15263 Genomic DNA. Translation: AAA23462.1.
J01641 Genomic DNA. Translation: AAA23467.1.
U00096 Genomic DNA. Translation: AAC73174.1.
AP009048 Genomic DNA. Translation: BAB96632.2.
K01304 mRNA. Translation: AAA23465.1.
PIRKIECRU. G64727.
RefSeqAP_000727.1.
NP_414605.1.

3D structure databases

SMRP08204. Positions 4-541.
ModBaseSearch...

Protein-protein interaction databases

IntActP08204. 1 interaction.
STRINGP08204.

2-D gel databases

ECO2DBASED055.0. 6TH EDITION.

Genome annotation databases

GeneID946017.
GenomeReviewsGene locus JW0062 in contig AP009048_GR.
Gene locus b0063 in contig U00096_GR.
KEGGecj:JW0062.
eco:b0063.

Organism-specific databases

EchoBASEEB0051.
EcoGeneEG10053. araB.
CMRSearch...

Phylogenomic databases

eggNOGCOG1069.
HOGENOMHBG312681.
OMANGRRTPD.

Enzyme and pathway databases

BioCycEcoCyc:RIBULOKIN-MONOMER.
ECOL168927:B0063-MONOMER.

Gene expression databases

GenevestigatorP08204.

Family and domain databases

HAMAPMF_00520. Ribulokinase.
[Tree]
InterProIPR000577. Carb_kinase_FGGY.
IPR018485. Carb_kinase_FGGY_C.
IPR018484. Carb_kinase_FGGY_N.
IPR005929. L_ribulokin.
[Graphical view]
PANTHERPTHR10196. FGGY_kin. 1 hit.
PfamPF02782. FGGY_C. 1 hit.
PF00370. FGGY_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01234. L-ribulokinase. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameARAB_ECOLI
AccessionPrimary (citable) accession number: P08204
Secondary accession number(s): P78041
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: February 9, 2010
This is version 87 of the entry and version 4 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

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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