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Q57843

- ADHS_METJA

UniProt

Q57843 - ADHS_METJA

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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: 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).2 PublicationsUniRule annotation

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.1 PublicationUniRule annotation

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

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei33 – 331Proton acceptorCurated
Active sitei153 – 1531Proton donorCurated
Active sitei184 – 1841Schiff-base intermediate with substrate

GO - Molecular functioni

  1. hydro-lyase activity Source: InterPro
  2. transferase activity, transferring aldehyde or ketonic groups Source: UniProtKB-HAMAP

GO - Biological processi

  1. aromatic amino acid family biosynthetic process Source: UniProtKB-HAMAP
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.
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
ProteomesiUP000000805: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2732732-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthasePRO_0000138957Add
BLAST

Interactioni

Subunit structurei

Homodecamer.1 PublicationUniRule annotation

Protein-protein interaction databases

STRINGi243232.MJ0400.

Structurei

Secondary structure

1
273
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 64Combined sources
Helixi10 – 167Combined sources
Turni17 – 193Combined sources
Turni22 – 243Combined sources
Beta strandi27 – 315Combined sources
Helixi34 – 385Combined sources
Beta strandi44 – 463Combined sources
Helixi47 – 5711Combined sources
Beta strandi60 – 645Combined sources
Helixi66 – 705Combined sources
Beta strandi75 – 773Combined sources
Beta strandi81 – 855Combined sources
Beta strandi93 – 953Combined sources
Helixi105 – 1106Combined sources
Beta strandi114 – 1229Combined sources
Helixi127 – 14418Combined sources
Beta strandi148 – 1547Combined sources
Helixi165 – 17713Combined sources
Beta strandi181 – 1855Combined sources
Helixi191 – 20010Combined sources
Beta strandi205 – 2084Combined sources
Helixi216 – 22914Combined sources
Beta strandi232 – 2354Combined sources
Helixi238 – 2414Combined sources
Beta strandi243 – 2453Combined sources
Helixi246 – 25914Combined sources
Helixi263 – 2675Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-272.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ57843.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 375DKFP binding
Regioni153 – 1553DKFP binding
Regioni209 – 2102DKFP binding
Regioni237 – 2382DKFP binding

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1830.
InParanoidiQ57843.
KOiK16306.
OMAiGNPYNAT.
PhylomeDBiQ57843.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00960. ADH_synthase.
InterProiIPR010210. ADH_synthase.
IPR013785. Aldolase_TIM.
IPR002915. DeoC/FbaB/lacD_aldolase.
[Graphical view]
PfamiPF01791. DeoC. 1 hit.
[Graphical view]
PIRSFiPIRSF038992. Aldolase_Ia. 1 hit.
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.
RefSeqiNP_247374.1. 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 .
PIRi H64349.
RefSeqi NP_247374.1. NC_000909.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2QJG X-ray 2.60 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T 1-273 [» ]
2QJH X-ray 2.60 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T 1-273 [» ]
2QJI X-ray 2.80 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T 1-273 [» ]
ProteinModelPortali Q57843.
SMRi Q57843. Positions 1-272.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243232.MJ0400.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB98389 ; AAB98389 ; MJ_0400 .
GeneIDi 1451260.
KEGGi mja:MJ_0400.

Phylogenomic databases

eggNOGi COG1830.
InParanoidi Q57843.
KOi K16306.
OMAi GNPYNAT.
PhylomeDBi Q57843.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-14592.
SABIO-RK Q57843.

Miscellaneous databases

EvolutionaryTracei Q57843.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00960. ADH_synthase.
InterProi IPR010210. ADH_synthase.
IPR013785. Aldolase_TIM.
IPR002915. DeoC/FbaB/lacD_aldolase.
[Graphical view ]
Pfami PF01791. DeoC. 1 hit.
[Graphical view ]
PIRSFi PIRSF038992. Aldolase_Ia. 1 hit.
TIGRFAMsi TIGR01949. AroFGH_arch. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

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 26, 2014
This is version 85 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

External Data

Dasty 3