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Reviewed, UniProtKB/Swiss-Prot Q9WYH8 (AROF_THEMA)

Last modified November 3, 2009. Version 62. 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:
    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: aroF
Ordered Locus Names: TM_0343
OrganismThermotoga maritima [Complete proteome] [HAMAP]
Taxonomic identifier2336 [NCBI]
Taxonomic lineageBacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

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Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes the condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).

Catalytic activity

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

Cofactor

Divalent ions.

Enzyme regulation

Inhibited by L-phenylalanine and L-tyrosine.

Pathway

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

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the class-I DAHP synthetase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.3 at 60 degrees Celsius.

Temperature dependence:

Optimum temperature is 90 degrees Celsius. Extremely thermostable.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 338338Phospho-2-dehydro-3-deoxyheptonate aldolase
PRO_0000140847

Secondary structure

1 ................................................................. 338
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q9WYH8-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: E9634B6704D3DF4D

FASTA33837,378
        10         20         30         40         50         60 
MIVVLKPGST EEDIRKVVKL AESYNLKCHI SKGQERTVIG IIGDDRYVVA DKFESLDCVE 

        70         80         90        100        110        120 
SVVRVLKPYK LVSREFHPED TVIDLGDVKI GNGYFTIIAG PCSVEGREML METAHFLSEL 

       130        140        150        160        170        180 
GVKVLRGGAY KPRTSPYSFQ GLGEKGLEYL REAADKYGMY VVTEALGEDD LPKVAEYADI 

       190        200        210        220        230        240 
IQIGARNAQN FRLLSKAGSY NKPVLLKRGF MNTIEEFLLS AEYIANSGNT KIILCERGIR 

       250        260        270        280        290        300 
TFEKATRNTL DISAVPIIRK ESHLPILVDP SHSGGRRDLV IPLSRAAIAV GAHGIIVEVH 

       310        320        330 
PEPEKALSDG KQSLDFELFK ELVQEMKKLA DALGVKVN

« Hide

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Cross-references

Sequence databases

AE000512 Genomic DNA. Translation: AAD35429.1.
PIRE72388.
RefSeqNP_228154.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1RZMX-ray2.20A/B1-338[»]
1VR6X-ray1.92A/B/C/D1-338[»]
ModBaseSearch...

Genome annotation databases

GeneID897299.
GenomeReviewsGene locus TM_0343 in contig AE000512_GR.
KEGGtma:TM0343.
NMPDRfig|243274.1.peg.338.
TIGRTM_0343.

Phylogenomic databases

HOGENOMQ9WYH8.
OMANDPANAL.

Enzyme and pathway databases

BioCycTMAR243274:TM_0343-MON.
BRENDA2.5.1.54. 16699.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR006218. DAHP1/KDSA.
IPR006268. DAHP_syn_2.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR21057:SF1. DAHP_syn_2. 1 hit.
PfamPF00793. DAHP_synth_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR01361. DAHP_synth_Bsub. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameAROF_THEMA
AccessionPrimary (citable) accession number: Q9WYH8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: November 1, 1999
Last modified: November 3, 2009
This is version 62 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