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Q9SA18 (AKH1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 104. 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:
Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic

Short name=AK-HD 1
Short name=AK-HSDH 1
Alternative name(s):
Beta-aspartyl phosphate homoserine 1

Including the following 2 domains:

  1. Aspartokinase
    EC=2.7.2.4
  2. Homoserine dehydrogenase
    EC=1.1.1.3
Gene names
Name:AKHSDH1
Synonyms:AK-HSDH I
Ordered Locus Names:At1g31230
ORF Names:F28K20.19, T19E23.1
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length911 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.6

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3.

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.

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

Plastidchloroplast.

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) Ref.6

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 8282Chloroplast Potential
Chain83 – 911829Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic
PRO_0000245844

Regions

Domain407 – 48276ACT 1
Domain488 – 56578ACT 2
Nucleotide binding559 – 5646NADP Potential
Region83 – 331249Aspartokinase By similarity
Region332 – 557226Interface By similarity
Region558 – 911354Homoserine dehydrogenase By similarity

Experimental info

Sequence conflict5171I → M in BAC43372. Ref.4
Sequence conflict9001I → F in BAC43372. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9SA18 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 95A663413B68585F

FASTA91199,404
        10         20         30         40         50         60 
MPVVSLAKVV TSPAVAGDLA VRVPFIYGKR LVSNRVSFGK LRRRSCIGQC VRSELQSPRV 

        70         80         90        100        110        120 
LGSVTDLALD NSVENGHLPK GDSWAVHKFG GTCVGNSERI KDVAAVVVKD DSERKLVVVS 

       130        140        150        160        170        180 
AMSKVTDMMY DLIHRAESRD DSYLSALSGV LEKHRATAVD LLDGDELSSF LARLNDDINN 

       190        200        210        220        230        240 
LKAMLRAIYI AGHATESFSD FVVGHGELWS AQMLAAVVRK SGLDCTWMDA RDVLVVIPTS 

       250        260        270        280        290        300 
SNQVDPDFVE SEKRLEKWFT QNSAKIIIAT GFIASTPQNI PTTLKRDGSD FSAAIMSALF 

       310        320        330        340        350        360 
RSHQLTIWTD VDGVYSADPR KVSEAVVLKT LSYQEAWEMS YFGANVLHPR TIIPVMKYDI 

       370        380        390        400        410        420 
PIVIRNIFNL SAPGTMICRQ IDDEDGFKLD APVKGFATID NLALVNVEGT GMAGVPGTAS 

       430        440        450        460        470        480 
AIFSAVKEVG ANVIMISQAS SEHSVCFAVP EKEVKAVSEA LNSRFRQALA GGRLSQIEII 

       490        500        510        520        530        540 
PNCSILAAVG QKMASTPGVS ATFFNALAKA NINIRAIAQG CSEFNITVVV KREDCIRALR 

       550        560        570        580        590        600 
AVHSRFYLSR TTLAVGIIGP GLIGGTLLDQ IRDQAAVLKE EFKIDLRVIG ITGSSKMLMS 

       610        620        630        640        650        660 
ESGIDLSRWR ELMKEEGEKA DMEKFTQYVK GNHFIPNSVM VDCTADADIA SCYYDWLLRG 

       670        680        690        700        710        720 
IHVVTPNKKA NSGPLDQYLK IRDLQRKSYT HYFYEATVGA GLPIISTLRG LLETGDKILR 

       730        740        750        760        770        780 
IEGIFSGTLS YLFNNFVGTR SFSEVVAEAK QAGFTEPDPR DDLSGTDVAR KVTILARESG 

       790        800        810        820        830        840 
LKLDLEGLPV QNLVPKPLQA CASAEEFMEK LPQFDEELSK QREEAEAAGE VLRYVGVVDA 

       850        860        870        880        890        900 
VEKKGTVELK RYKKDHPFAQ LSGADNIIAF TTKRYKEQPL IVRGPGAGAQ VTAGGIFSDI 

       910 
LRLAFYLGAP S 

« Hide

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. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-573.
Strain: cv. Columbia.
[6]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC004793 Genomic DNA. Translation: AAD21689.1.
AC007654 Genomic DNA. Translation: AAF24602.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE31330.1.
AK118779 mRNA. Translation: BAC43372.1.
X71364 Genomic DNA. Translation: CAA50500.2. Sequence problems.
PIRE86438.
S46497.
RefSeqNP_174408.1. NM_102861.3.
UniGeneAt.48251.
At.71214.

3D structure databases

ProteinModelPortalQ9SA18.
SMRQ9SA18. Positions 86-546, 549-904.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid25246. 1 interaction.
MINTMINT-8067838.

Proteomic databases

PaxDbQ9SA18.
PRIDEQ9SA18.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G31230.1; AT1G31230.1; AT1G31230.
GeneID840011.
KEGGath:AT1G31230.

Organism-specific databases

TAIRAT1G31230.

Phylogenomic databases

eggNOGCOG0527.
HOGENOMHOG000271593.
InParanoidQ9SA18.
KOK12524.
OMAASACEIW.
PhylomeDBQ9SA18.

Enzyme and pathway databases

SABIO-RKQ9SA18.
UniPathwayUPA00034; UER00015.
UPA00050; UER00063.
UPA00050; UER00461.
UPA00051; UER00462.
UPA00051; UER00465.

Gene expression databases

GenevestigatorQ9SA18.

Family and domain databases

Gene3D3.40.1160.10. 2 hits.
3.40.50.720. 1 hit.
InterProIPR002912. ACT_dom.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR005106. Asp/hSer_DH_NAD-bd.
IPR001341. Asp_kinase_dom.
IPR018042. Aspartate_kinase_CS.
IPR011147. Bifunc_aspartokin/hSer_DH.
IPR001342. HDH_cat.
IPR019811. HDH_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00696. AA_kinase. 1 hit.
PF01842. ACT. 2 hits.
PF00742. Homoserine_dh. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFPIRSF000727. ThrA. 1 hit.
SUPFAMSSF53633. SSF53633. 1 hit.
TIGRFAMsTIGR00657. asp_kinases. 1 hit.
PROSITEPS51671. ACT. 2 hits.
PS00324. ASPARTOKINASE. 1 hit.
PS01042. HOMOSER_DHGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAKH1_ARATH
AccessionPrimary (citable) accession number: Q9SA18
Secondary accession number(s): Q8GWK9, Q9SHF9, Q9SW59
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names