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Reviewed, UniProtKB/Swiss-Prot Q57843 (ADHS_METJA)

Last modified February 9, 2010. Version 55. 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

Names and origin

Protein namesRecommended name:
    2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase
      Short name=ADH synthase
      Short name=ADHS
    EC=4.1.2.n5
Alternative name(s):
    Transaldolase-like ADHS
Gene names
Ordered Locus Names: MJ0400
OrganismMethanocaldococcus jannaschii (Methanococcus jannaschii) [Complete proteome] [HAMAP]
Taxonomic identifier2190 [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-ulosonic acid (ADH). Play 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 semialdehyde + 6-deoxy-5-ketofructose 1-phosphate = hydroxypyruvaldehyde phosphate+ 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate.

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)

Vmax=33 nmol/min/mg enzyme (at pH 7 and 50 degrees Celsius)

Temperature dependence:

Optimum temperature is not reached at 100 degrees Celsius.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

Region33 – 375DKFP binding
Region153 – 1553DKFP binding
Region209 – 2102DKFP binding
Region237 – 2382DKFP binding

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
Q57843-1 [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: 8688087] [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: 15182204] [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: 18318840] [Abstract]
Cited for: FUNCTION AS A FBP ALDOLASE, 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: 17713928] [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.

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[»]
ModBaseSearch...

Genome annotation databases

GeneID1451260.
GenomeReviewsGene locus MJ0400 in contig L77117_GR.
KEGGmja:MJ0400.
NMPDRfig|243232.1.peg.411.
TIGRMJ0400.

Phylogenomic databases

HOGENOMHBG553580.
OMAVRHGHRG.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14592.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR010210. AroFGH_arch.
IPR002915. DeoC/AroFGH_arch.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PfamPF01791. DeoC. 1 hit.
[Graphical view]
TIGRFAMsTIGR01949. AroFGH_arch. 1 hit.
ProtoNetSearch...

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 9, 2010
This is version 55 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)

Relevant documents

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names

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