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Reviewed, UniProtKB/Swiss-Prot P80574 (AROF_STRCO)

Last modified November 3, 2009. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
    Phospho-2-dehydro-3-deoxyheptonate aldolase
    EC=2.5.1.54
Alternative name(s):
    Phospho-2-keto-3-deoxyheptonate aldolase
    3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
    DAHP synthetase
Gene names
Name: aroH
Ordered Locus Names: SCO2115
ORF Names: SC6E10.09c
OrganismStreptomyces coelicolor [Complete proteome] [HAMAP]
Taxonomic identifier1902 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate.

Pathway

Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the class-II DAHP synthetase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 450449Phospho-2-dehydro-3-deoxyheptonate aldolase
PRO_0000140854

Experimental info

Sequence conflict15 – 228WRDLPAAQ → DDPLQAPS AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P80574-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 074668C290250874

FASTA45049,870
        10         20         30         40         50         60 
MTVNAKTSPS AGNTWRDLPA AQQPEYPDTE ALRAVIADLE SYPPLVFAGE CDQLRARMAA 

        70         80         90        100        110        120 
VAKGEAFLLQ GGDCAEAFDA VSADHIRNKL KTLLQMGAVL TYAASVPVVK VGRIAGQYSK 

       130        140        150        160        170        180 
PRSKPTETRD GVTLPTYRGD SVNGFDFTEA ARIPDPERLK RMYHASASTL NLVRAFTTGG 

       190        200        210        220        230        240 
YADLRQVHAW NQDFVKSSPS GQRYEQLARE IDNALNFMRA CGTDPAEFQT VEFFSSHEAL 

       250        260        270        280        290        300 
LLDYESALTR VDSRTGQLYD VSGHMVWIGE RTRQLDHAHI EFASRIRNPI GIKLGPSTTA 

       310        320        330        340        350        360 
EEALQYIERL DPEREPGRLT FIVRMGADKI RDKLPELVEK VTASGATVAW ITDPMHGNTY 

       370        380        390        400        410        420 
EAASGHKTRR FDDVLDEVKG FFEVHKSLGT HPGGIHVELT GDDVTECVGG GDEIFVDDLH 

       430        440        450 
QRYETACDPR LNRSQSLDLA FLVAEMYRDQ 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)."
Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. expand/collapse author list , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.
Nature 417:141-147(2002) [PubMed: 12000953] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-471 / A3(2) / M145.
[2]"Evidence for a novel class of microbial 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase in Streptomyces coelicolor A3(2), Streptomyces rimosus and Neurospora crassa."
Walker G.E., Dunbar B., Hunter I.S., Nimmo H.G., Coggins J.R.
Microbiology 142:1973-1982(1996) [PubMed: 8760910] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-22, CHARACTERIZATION.
Strain: A3(2).

Cross-references

Sequence databases

AL939111 Genomic DNA. Translation: CAB51963.1.
PIRT35496.
RefSeqNP_626372.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1097549.
GenomeReviewsGene locus SCO2115 in contig AL645882_GR.
KEGGsco:SCO2115.
NMPDRfig|100226.1.peg.2081.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP80574.
OMAYDTSAHF.

Enzyme and pathway databases

BioCycSCOE100226:SCO2115-MON.
BRENDA2.5.1.54. 1084.

Family and domain databases

InterProIPR002480. DAHP_synth_2.
[Graphical view]
PANTHERPTHR21337. DAHP_synth_2. 1 hit.
PfamPF01474. DAHP_synth_2. 1 hit.
[Graphical view]
TIGRFAMsTIGR01358. DAHP_synth_II. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAROF_STRCO
AccessionPrimary (citable) accession number: P80574
Secondary accession number(s): Q9S2M8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: November 3, 2009
This is version 60 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents