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Protein

Phospho-2-dehydro-3-deoxyheptonate aldolase

Gene

aroF

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

a divalent metal cationNote: Divalent metal ions.

Enzyme regulationi

Inhibited by L-phenylalanine and L-tyrosine.

pH dependencei

Optimum pH is 6.3 at 60 degrees Celsius.

Temperature dependencei

Optimum temperature is 90 degrees Celsius. Extremely thermostable.

Pathway: chorismate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. Phospho-2-dehydro-3-deoxyheptonate aldolase (aroF)
  2. Bifunctional shikimate kinase/3-dehydroquinate synthase (aroKB)
  3. 3-dehydroquinate dehydratase (aroQ)
  4. Shikimate 5-dehydrogenase I alpha (Tmari_0344), Shikimate dehydrogenase (NADP(+)) (aroE)
  5. Bifunctional shikimate kinase/3-dehydroquinate synthase (aroKB), Shikimate kinase I / 3-dehydroquinate synthase (Tmari_0346)
  6. 3-phosphoshikimate 1-carboxyvinyltransferase (aroA)
  7. Chorismate synthase (aroC)
This subpathway is part of the pathway chorismate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate, the pathway chorismate biosynthesis and in Metabolic intermediate biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00053; UER00084.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospho-2-dehydro-3-deoxyheptonate aldolase (EC:2.5.1.54)
Alternative name(s):
3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
DAHP synthase
Phospho-2-keto-3-deoxyheptonate aldolase
Gene namesi
Name:aroF
Ordered Locus Names:TM_0343
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000008183 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 338338Phospho-2-dehydro-3-deoxyheptonate aldolasePRO_0000140847Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi243274.TM0343.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 55Combined sources
Helixi11 – 2313Combined sources
Beta strandi26 – 327Combined sources
Beta strandi37 – 4711Combined sources
Helixi50 – 545Combined sources
Beta strandi59 – 646Combined sources
Turni74 – 763Combined sources
Beta strandi82 – 843Combined sources
Beta strandi89 – 913Combined sources
Beta strandi94 – 1007Combined sources
Helixi107 – 11913Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi128 – 1303Combined sources
Helixi144 – 15714Combined sources
Beta strandi160 – 1645Combined sources
Helixi168 – 1703Combined sources
Helixi171 – 1777Combined sources
Beta strandi179 – 1835Combined sources
Helixi185 – 1873Combined sources
Helixi191 – 1988Combined sources
Beta strandi204 – 2074Combined sources
Helixi214 – 22613Combined sources
Beta strandi232 – 2365Combined sources
Beta strandi245 – 2495Combined sources
Helixi254 – 2618Combined sources
Beta strandi262 – 2643Combined sources
Beta strandi266 – 2683Combined sources
Helixi270 – 2745Combined sources
Helixi277 – 2793Combined sources
Helixi280 – 29011Combined sources
Beta strandi293 – 2997Combined sources
Helixi303 – 3053Combined sources
Helixi310 – 3123Combined sources
Helixi316 – 33318Combined sources
Beta strandi336 – 3383Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RZMX-ray2.20A/B1-338[»]
1VR6X-ray1.92A/B/C/D1-338[»]
3PG8X-ray2.00A/B71-338[»]
3PG9X-ray2.35A/B/C/D/E/F/G/H1-338[»]
4GRSX-ray3.00A/B/C/D1-103[»]
ProteinModelPortaliQ9WYH8.
SMRiQ9WYH8. Positions 1-338.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WYH8.

Family & Domainsi

Sequence similaritiesi

Belongs to the class-I DAHP synthase family.Curated

Phylogenomic databases

eggNOGiCOG2876.
InParanoidiQ9WYH8.
KOiK03856.
OMAiMVIVMAP.
OrthoDBiEOG657JFQ.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006218. DAHP1/KDSA.
IPR006268. DAHP_syn_2.
[Graphical view]
PfamiPF00793. DAHP_synth_1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01361. DAHP_synth_Bsub. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9WYH8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIVVLKPGST EEDIRKVVKL AESYNLKCHI SKGQERTVIG IIGDDRYVVA
60 70 80 90 100
DKFESLDCVE SVVRVLKPYK LVSREFHPED TVIDLGDVKI GNGYFTIIAG
110 120 130 140 150
PCSVEGREML METAHFLSEL GVKVLRGGAY KPRTSPYSFQ GLGEKGLEYL
160 170 180 190 200
REAADKYGMY VVTEALGEDD LPKVAEYADI IQIGARNAQN FRLLSKAGSY
210 220 230 240 250
NKPVLLKRGF MNTIEEFLLS AEYIANSGNT KIILCERGIR TFEKATRNTL
260 270 280 290 300
DISAVPIIRK ESHLPILVDP SHSGGRRDLV IPLSRAAIAV GAHGIIVEVH
310 320 330
PEPEKALSDG KQSLDFELFK ELVQEMKKLA DALGVKVN
Length:338
Mass (Da):37,378
Last modified:November 1, 1999 - v1
Checksum:iE9634B6704D3DF4D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35429.1.
PIRiE72388.
RefSeqiNP_228154.1. NC_000853.1.
WP_004083125.1. NC_023151.1.
YP_007976691.1. NC_021214.1.
YP_008990684.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD35429; AAD35429; TM_0343.
GeneIDi897299.
KEGGitma:TM0343.
tmi:THEMA_03000.
tmm:Tmari_0341.
PATRICi23935567. VBITheMar51294_0348.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35429.1.
PIRiE72388.
RefSeqiNP_228154.1. NC_000853.1.
WP_004083125.1. NC_023151.1.
YP_007976691.1. NC_021214.1.
YP_008990684.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RZMX-ray2.20A/B1-338[»]
1VR6X-ray1.92A/B/C/D1-338[»]
3PG8X-ray2.00A/B71-338[»]
3PG9X-ray2.35A/B/C/D/E/F/G/H1-338[»]
4GRSX-ray3.00A/B/C/D1-103[»]
ProteinModelPortaliQ9WYH8.
SMRiQ9WYH8. Positions 1-338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM0343.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD35429; AAD35429; TM_0343.
GeneIDi897299.
KEGGitma:TM0343.
tmi:THEMA_03000.
tmm:Tmari_0341.
PATRICi23935567. VBITheMar51294_0348.

Phylogenomic databases

eggNOGiCOG2876.
InParanoidiQ9WYH8.
KOiK03856.
OMAiMVIVMAP.
OrthoDBiEOG657JFQ.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00084.

Miscellaneous databases

EvolutionaryTraceiQ9WYH8.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006218. DAHP1/KDSA.
IPR006268. DAHP_syn_2.
[Graphical view]
PfamiPF00793. DAHP_synth_1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01361. DAHP_synth_Bsub. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  2. "Thermotoga maritima 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase: the ancestral eubacterial DAHP synthase?"
    Wu J., Howe D.L., Woodard R.W.
    J. Biol. Chem. 278:27525-27531(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

Entry informationi

Entry nameiAROF_THEMA
AccessioniPrimary (citable) accession number: Q9WYH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: November 1, 1999
Last modified: May 27, 2015
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.