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Q57843 (ADHS_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase

Short name=ADH synthase
Short name=ADHS
Short name=ADTH synthase
EC=2.2.1.10
Alternative name(s):
Transaldolase-like ADHS
Gene names
Name:aroA'
Ordered Locus Names:MJ0400
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus

Protein attributes

Sequence length273 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids. Can also catalyze the cleavage of fructose-1,6-bisphosphate (FBP) to glyceraldehyde-3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP). Ref.2 Ref.3

Catalytic activity

L-aspartate 4-semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + 2,3-dioxopropylaldehyde phosphate. Ref.3

Enzyme regulation

Inhibited by NaBH4 in the presence of FBP. Ref.3

Subunit structure

Homodecamer. Ref.4

Sequence similarities

Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=430 µM for fructose-1,6-bisphosphate (at pH 7 and 50 degrees Celsius) Ref.3

Vmax=33 nmol/min/mg enzyme for the FBP aldolase activity (at pH 7 and 50 degrees Celsius)

Temperature dependence:

Optimum temperature is not reached at 100 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2732732-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase HAMAP-Rule MF_00960
PRO_0000138957

Regions

Region33 – 375DKFP binding HAMAP-Rule MF_00960
Region153 – 1553DKFP binding HAMAP-Rule MF_00960
Region209 – 2102DKFP binding HAMAP-Rule MF_00960
Region237 – 2382DKFP binding HAMAP-Rule MF_00960

Sites

Active site331Proton acceptor Probable
Active site1531Proton donor Probable
Active site1841Schiff-base intermediate with substrate

Secondary structure

.................................................... 273
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q57843 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 06DDA2E51E8275E6

FASTA27329,675
        10         20         30         40         50         60 
MELFKDIKNL GKLVRLERIF NRESEKTVIV PMDHGVSNGP IKGLIDIRKT VNDVAEGGAN 

        70         80         90        100        110        120 
AVLLHKGIVR HGHRGYGKDV GLIIHLSGGT AISPNPLKKV IVTTVEEAIR MGADAVSIHV 

       130        140        150        160        170        180 
NVGSDEDWEA YRDLGMIAET CEYWGMPLIA MMYPRGKHIQ NERDPELVAH AARLGAELGA 

       190        200        210        220        230        240 
DIVKTSYTGD IDSFRDVVKG CPAPVVVAGG PKTNTDEEFL QMIKDAMEAG AAGVAVGRNI 

       250        260        270 
FQHDDVVGIT RAVCKIVHEN ADVEEALKEI RKK 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii."
Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. expand/collapse author list , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
Science 273:1058-1073(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]"L-aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus jannaschii."
White R.H.
Biochemistry 43:7618-7627(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS AN ADH SYNTHASE.
[3]"MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity."
Samland A.K., Wang M., Sprenger G.A.
FEMS Microbiol. Lett. 281:36-41(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A FBP ALDOLASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[4]"Structure of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, a catalyst in the archaeal pathway for the biosynthesis of aromatic amino acids."
Morar M., White R.H., Ealick S.E.
Biochemistry 46:10562-10571(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, REACTION MECHANISM, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77117 Genomic DNA. Translation: AAB98389.1.
PIRH64349.
RefSeqNP_247374.1. NC_000909.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QJGX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-273[»]
2QJHX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-273[»]
2QJIX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-273[»]
ProteinModelPortalQ57843.
SMRQ57843. Positions 1-272.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243232.MJ0400.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB98389; AAB98389; MJ_0400.
GeneID1451260.
KEGGmja:MJ_0400.

Phylogenomic databases

eggNOGCOG1830.
KOK16306.
OMACEYWGMP.
ProtClustDBPRK07226.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14592.
SABIO-RKQ57843.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00960. ADH_synthase.
InterProIPR010210. ADH_synthase.
IPR013785. Aldolase_TIM.
IPR002915. DeoC/FbaB/lacD_aldolase.
[Graphical view]
PfamPF01791. DeoC. 1 hit.
[Graphical view]
PIRSFPIRSF038992. Aldolase_Ia. 1 hit.
TIGRFAMsTIGR01949. AroFGH_arch. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ57843.

Entry information

Entry nameADHS_METJA
AccessionPrimary (citable) accession number: Q57843
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names