Reviewed,
UniProtKB/Swiss-Prot Q9SA18 (AKH1_ARATH)
Last modified
June 16, 2009.
Version 61.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic Short name=AK-HSDH 1 Short name=AK-HD 1 Alternative name(s): Beta-aspartyl phosphate homoserine 1 Including the following 2 domains: 1- Recommended name: Aspartokinase EC=2.7.2.4 2- Recommended name: Homoserine dehydrogenase EC=1.1.1.3 | ||||||||
| Gene names |
| ||||||||
| Organism | Arabidopsis thaliana (Mouse-ear cress) [Complete proteome] | ||||||||
| Taxonomic identifier | 3702 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis |
Protein attributes
| Sequence length | 911 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H. ATP + L-aspartate = ADP + 4-phospho-L-aspartate. |
| Enzyme regulation | Inhibition of aspartate kinase activity by threonine and leucine and 3-fold activation by cysteine, isoleucine, valine, serine and alanine at 2.5 mM. Partial inhibition of homoserine dehydrogenase activity by threonine and cysteine (14% of activity remaining at saturation with either amino acid). No synergy between the effectors for both activation or inhibition. Ref.5 |
| Pathway | Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 3/5. |
| Subunit structure | Homo- or heterodimer Potential. |
| Subcellular location | |
| Sequence similarities | In the N-terminal section; belongs to the aspartokinase family. In the C-terminal section; belongs to the homoserine dehydrogenase family. Contains 2 ACT domains. |
| biophysicochemical properties | Kinetic parameters: KM=2.6 mM for aspartate for the aspartokinase activity (at pH 8.0, in the presence of 150 mM KCl, 20 mM MgCl2, 200 µM NADPH and 20 mM ATP) KM=2.3 mM for aspartate for the aspartokinase activity (at pH 8.0, in the presence of 150 mM KCl, 20 mM MgCl2, 200 µM NADPH, 20 mM ATP and a saturating concentration of alanine) KM=6.5 mM for ATP for the aspartokinase activity (at pH 8.0, in the presence of 150 mM KCl, 20 mM MgCl2, 200 µM NADPH and 50 mM aspartate) KM=0.48 mM for ATP for the aspartokinase activity (at pH 8.0, in the presence of 150 mM KCl, 20 mM MgCl2, 200 µM NADPH, 50 mM aspartate and a saturating concentration of alanine) KM=290 µM for aspartate semialdehyde for the forward reaction of the homoserine dehydrogenase activity (at pH 8.0, in the presence of 150 mM KCl and 200 µM NADPH) |
| Sequence caution | The sequence AAF24602.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAA50500.2 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Methionine biosynthesis |
| Cellular component | Chloroplast Plastid |
| Domain | Repeat Transit peptide |
| Ligand | ATP-binding NADP Nucleotide-binding |
| Molecular function | Kinase Oxidoreductase Transferase |
| Technical term | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | chloroplast stroma Inferred from direct assay. Source: TAIR |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW NADP or NADPH bindingInferred from electronic annotation. Source: InterPro amino acid bindingInferred from electronic annotation. Source: InterPro aspartate kinase activity Ref.5Inferred from direct assay. Source: TAIR homoserine dehydrogenase activity Ref.5Inferred from direct assay. Source: TAIR |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 82 | 82 | Chloroplast Potential | ||||||
| Chain | 83 – 911 | 829 | Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic | PRO_0000245844 | |||||
Regions | |||||||||
| Domain | 403 – 471 | 69 | ACT 1 | ||||||
| Domain | 487 – 554 | 68 | ACT 2 | ||||||
| Nucleotide binding | 559 – 564 | 6 | NADP Potential | ||||||
| Region | 83 – 331 | 249 | Aspartokinase By similarity | ||||||
| Region | 332 – 557 | 226 | Interface By similarity | ||||||
| Region | 558 – 911 | 354 | Homoserine dehydrogenase By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 517 | 1 | I → M in BAC43372. Ref.3 | ||||||
| Sequence conflict | 900 | 1 | I → F in BAC43372. Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. Davis R.W.Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia. |
| [2] | "Overproduction, purification, and characterization of recombinant bifunctional threonine-sensitive aspartate kinase-homoserine dehydrogenase from Arabidopsis thaliana." Paris S., Wessel P.M., Dumas R. Protein Expr. Purif. 24:105-110(2002) [PubMed: 11812230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [3] | "Functional annotation of a full-length Arabidopsis cDNA collection." Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K. Science 296:141-145(2002) [PubMed: 11910074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia. |
| [4] | "Molecular analysis of the aspartate kinase-homoserine dehydrogenase gene from Arabidopsis thaliana." Ghislain M., Frankard V., Vandenbossche D., Matthews B., Jacobs M. Plant Mol. Biol. 24:835-851(1994) [PubMed: 8204822] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-573. Strain: cv. Columbia. |
| [5] | "Identification of six novel allosteric effectors of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase isoforms. Physiological context sets the specificity." Curien G., Ravanel S., Robert M., Dumas R. J. Biol. Chem. 280:41178-41183(2005) [PubMed: 16216875] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. |
Cross-references
Sequence databases | |
|---|---|
| AC004793 Genomic DNA. Translation: AAD21689.1. AC007654 Genomic DNA. Translation: AAF24602.1. Sequence problems. AK118779 mRNA. Translation: BAC43372.1. X71364 Genomic DNA. Translation: CAA50500.2. Sequence problems. | |
| IPI | IPI00531888. |
| PIR | E86438. S46497. |
| RefSeq | NP_174408.1. |
| UniGene | At.71214 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1EBF based on UniProtKB P31116. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | Q9SA18. |
| ProMEX | Q9SA18. |
Genome annotation databases | |
| GeneID | 840011. |
| GenomeReviews | Gene locus AT1G31230 in contig CT485782_GR. |
| KEGG | ath:AT1G31230. |
| NMPDR | fig|3702.1.peg.3465. |
Organism-specific databases | |
| TAIR | At1g31230. |
Phylogenomic databases | |
| OMA | Q9SA18. RYLARID. |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.3. 302. 2.7.2.4. 302. |
Gene expression databases | |
| GermOnline | AT1G31230. Arabidopsis thaliana. |
Family and domain databases | |
| InterPro | IPR002912. ACT_bd. IPR001048. Asp/Glu/Uridylate_kinase. IPR005106. Asp/hSer_DH_NAD-bd. IPR001341. Asp_kin_reg. IPR018042. Aspartate_kinase_CS. IPR011147. bifunc_aspartokin/hSer_DH. IPR001342. Homoserine_dehydrogenase_cat. IPR019811. Homoserine_dehydrogenase_CS. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.1160.10. Aa_kinase. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF00696. AA_kinase. 1 hit. PF01842. ACT. 2 hits. PF00742. Homoserine_dh. 1 hit. PF03447. NAD_binding_3. 1 hit. [Graphical view] |
| PIRSF | PIRSF000727. ThrA. 1 hit. |
| TIGRFAMs | TIGR00657. asp_kinases. 1 hit. |
| PROSITE | PS00324. ASPARTOKINASE. 1 hit. PS01042. HOMOSER_DHGENASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AKH1_ARATH | ||||||||
| Accession | Primary (citable) accession number: Q9SA18 Secondary accession number(s): Q8GWK9, Q9SHF9, Q9SW59 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


