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Protein

2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase

Gene

aroA'

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).UniRule annotation2 Publications

Catalytic activityi

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.UniRule annotation1 Publication

Enzyme regulationi

Inhibited by NaBH4 in the presence of FBP.1 Publication

Kineticsi

  1. KM=430 µM for fructose-1,6-bisphosphate (at pH 7 and 50 degrees Celsius)1 Publication
  1. Vmax=33 nmol/min/mg enzyme for the FBP aldolase activity (at pH 7 and 50 degrees Celsius)1 Publication

Temperature dependencei

Optimum temperature is not reached at 100 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei33Proton acceptor1 Publication1
Active sitei153Proton donor1 Publication1
Active sitei184Schiff-base intermediate with substrate1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14592.
BRENDAi2.2.1.10. 3260.
SABIO-RKQ57843.

Names & Taxonomyi

Protein namesi
Recommended name:
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthaseUniRule annotation (EC:2.2.1.10UniRule annotation)
Short name:
ADH synthaseUniRule annotation
Short name:
ADHSUniRule annotation
Short name:
ADTH synthaseUniRule annotation
Alternative name(s):
Transaldolase-like ADHS
Gene namesi
Name:aroA'UniRule annotation
Ordered Locus Names:MJ0400
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
Proteomesi
  • UP000000805 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001389571 – 2732-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthaseAdd BLAST273

Interactioni

Subunit structurei

Homodecamer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi243232.MJ_0400.

Structurei

Secondary structure

1273
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni3 – 6Combined sources4
Helixi10 – 16Combined sources7
Turni17 – 19Combined sources3
Turni22 – 24Combined sources3
Beta strandi27 – 31Combined sources5
Helixi34 – 38Combined sources5
Beta strandi44 – 46Combined sources3
Helixi47 – 57Combined sources11
Beta strandi60 – 64Combined sources5
Helixi66 – 70Combined sources5
Beta strandi75 – 77Combined sources3
Beta strandi81 – 85Combined sources5
Beta strandi93 – 95Combined sources3
Helixi105 – 110Combined sources6
Beta strandi114 – 122Combined sources9
Helixi127 – 144Combined sources18
Beta strandi148 – 154Combined sources7
Helixi165 – 177Combined sources13
Beta strandi181 – 185Combined sources5
Helixi191 – 200Combined sources10
Beta strandi205 – 208Combined sources4
Helixi216 – 229Combined sources14
Beta strandi232 – 235Combined sources4
Helixi238 – 241Combined sources4
Beta strandi243 – 245Combined sources3
Helixi246 – 259Combined sources14
Helixi263 – 267Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ57843.
SMRiQ57843.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ57843.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 37DKFP binding1 Publication5
Regioni153 – 155DKFP binding1 Publication3
Regioni209 – 210DKFP binding1 Publication2
Regioni237 – 238DKFP binding1 Publication2

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiarCOG04044. Archaea.
COG1830. LUCA.
InParanoidiQ57843.
KOiK16306.
OMAiIVRHGHR.
PhylomeDBiQ57843.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00960. ADH_synthase. 1 hit.
InterProiIPR010210. ADH_synthase.
IPR013785. Aldolase_TIM.
IPR002915. DeoC/FbaB/lacD_aldolase.
[Graphical view]
PfamiPF01791. DeoC. 1 hit.
[Graphical view]
PIRSFiPIRSF038992. Aldolase_Ia. 1 hit.
SMARTiSM01133. DeoC. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01949. AroFGH_arch. 1 hit.

Sequencei

Sequence statusi: Complete.

Q57843-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELFKDIKNL GKLVRLERIF NRESEKTVIV PMDHGVSNGP IKGLIDIRKT
60 70 80 90 100
VNDVAEGGAN AVLLHKGIVR HGHRGYGKDV GLIIHLSGGT AISPNPLKKV
110 120 130 140 150
IVTTVEEAIR MGADAVSIHV NVGSDEDWEA YRDLGMIAET CEYWGMPLIA
160 170 180 190 200
MMYPRGKHIQ NERDPELVAH AARLGAELGA DIVKTSYTGD IDSFRDVVKG
210 220 230 240 250
CPAPVVVAGG PKTNTDEEFL QMIKDAMEAG AAGVAVGRNI FQHDDVVGIT
260 270
RAVCKIVHEN ADVEEALKEI RKK
Length:273
Mass (Da):29,675
Last modified:November 1, 1996 - v1
Checksum:i06DDA2E51E8275E6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98389.1.
PIRiH64349.
RefSeqiWP_010869899.1. NC_000909.1.

Genome annotation databases

EnsemblBacteriaiAAB98389; AAB98389; MJ_0400.
GeneIDi1451260.
KEGGimja:MJ_0400.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98389.1.
PIRiH64349.
RefSeqiWP_010869899.1. NC_000909.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ57843.
SMRiQ57843.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_0400.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB98389; AAB98389; MJ_0400.
GeneIDi1451260.
KEGGimja:MJ_0400.

Phylogenomic databases

eggNOGiarCOG04044. Archaea.
COG1830. LUCA.
InParanoidiQ57843.
KOiK16306.
OMAiIVRHGHR.
PhylomeDBiQ57843.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14592.
BRENDAi2.2.1.10. 3260.
SABIO-RKQ57843.

Miscellaneous databases

EvolutionaryTraceiQ57843.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00960. ADH_synthase. 1 hit.
InterProiIPR010210. ADH_synthase.
IPR013785. Aldolase_TIM.
IPR002915. DeoC/FbaB/lacD_aldolase.
[Graphical view]
PfamiPF01791. DeoC. 1 hit.
[Graphical view]
PIRSFiPIRSF038992. Aldolase_Ia. 1 hit.
SMARTiSM01133. DeoC. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01949. AroFGH_arch. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiADHS_METJA
AccessioniPrimary (citable) accession number: Q57843
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 99 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. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.