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Protein

Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic

Gene

AKHSDH1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H.
ATP + L-aspartate = ADP + 4-phospho-L-aspartate.

Enzyme regulationi

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.1 Publication

Kineticsi

  1. 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)1 Publication
  2. 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)1 Publication
  3. 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)1 Publication
  4. 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)1 Publication
  5. 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)1 Publication

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi559 – 5646NADPSequence Analysis

GO - Molecular functioni

  1. amino acid binding Source: InterPro
  2. aspartate kinase activity Source: TAIR
  3. ATP binding Source: UniProtKB-KW
  4. homoserine dehydrogenase activity Source: TAIR
  5. NADP binding Source: InterPro

GO - Biological processi

  1. lysine biosynthetic process via diaminopimelate Source: UniProtKB-UniPathway
  2. methionine biosynthetic process Source: UniProtKB-KW
  3. threonine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Oxidoreductase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Keywords - Ligandi

ATP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKQ9SA18.
UniPathwayiUPA00034; UER00015.
UPA00050; UER00063.
UPA00050; UER00461.
UPA00051; UER00462.
UPA00051; UER00465.

Names & Taxonomyi

Protein namesi
Recommended 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:
Aspartokinase (EC:2.7.2.4)
Homoserine dehydrogenase (EC:1.1.1.3)
Gene namesi
Name:AKHSDH1
Synonyms:AK-HSDH I
Ordered Locus Names:At1g31230
ORF Names:F28K20.19, T19E23.1
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G31230.

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. chloroplast stroma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 8282ChloroplastSequence AnalysisAdd
BLAST
Chaini83 – 911829Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplasticPRO_0000245844Add
BLAST

Proteomic databases

PaxDbiQ9SA18.
PRIDEiQ9SA18.

Expressioni

Gene expression databases

GenevestigatoriQ9SA18.

Interactioni

Subunit structurei

Homo- or heterodimer.Curated

Protein-protein interaction databases

BioGridi25246. 1 interaction.
IntActiQ9SA18. 1 interaction.
MINTiMINT-8067838.

Structurei

3D structure databases

ProteinModelPortaliQ9SA18.
SMRiQ9SA18. Positions 86-546, 549-904.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini407 – 48276ACT 1PROSITE-ProRule annotationAdd
BLAST
Domaini488 – 56578ACT 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni83 – 331249AspartokinaseBy similarityAdd
BLAST
Regioni332 – 557226InterfaceBy similarityAdd
BLAST
Regioni558 – 911354Homoserine dehydrogenaseBy similarityAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the aspartokinase family.Curated
In the C-terminal section; belongs to the homoserine dehydrogenase family.Curated
Contains 2 ACT domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

eggNOGiCOG0527.
HOGENOMiHOG000271593.
InParanoidiQ9SA18.
KOiK12524.
OMAiPIEMRHD.
PhylomeDBiQ9SA18.

Family and domain databases

Gene3Di3.40.1160.10. 2 hits.
3.40.50.720. 1 hit.
InterProiIPR002912. 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]
PfamiPF00696. AA_kinase. 1 hit.
PF01842. ACT. 2 hits.
PF00742. Homoserine_dh. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000727. ThrA. 1 hit.
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00657. asp_kinases. 1 hit.
PROSITEiPS51671. ACT. 2 hits.
PS00324. ASPARTOKINASE. 1 hit.
PS01042. HOMOSER_DHGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9SA18-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPVVSLAKVV TSPAVAGDLA VRVPFIYGKR LVSNRVSFGK LRRRSCIGQC
60 70 80 90 100
VRSELQSPRV LGSVTDLALD NSVENGHLPK GDSWAVHKFG GTCVGNSERI
110 120 130 140 150
KDVAAVVVKD DSERKLVVVS AMSKVTDMMY DLIHRAESRD DSYLSALSGV
160 170 180 190 200
LEKHRATAVD LLDGDELSSF LARLNDDINN LKAMLRAIYI AGHATESFSD
210 220 230 240 250
FVVGHGELWS AQMLAAVVRK SGLDCTWMDA RDVLVVIPTS SNQVDPDFVE
260 270 280 290 300
SEKRLEKWFT QNSAKIIIAT GFIASTPQNI PTTLKRDGSD FSAAIMSALF
310 320 330 340 350
RSHQLTIWTD VDGVYSADPR KVSEAVVLKT LSYQEAWEMS YFGANVLHPR
360 370 380 390 400
TIIPVMKYDI PIVIRNIFNL SAPGTMICRQ IDDEDGFKLD APVKGFATID
410 420 430 440 450
NLALVNVEGT GMAGVPGTAS AIFSAVKEVG ANVIMISQAS SEHSVCFAVP
460 470 480 490 500
EKEVKAVSEA LNSRFRQALA GGRLSQIEII PNCSILAAVG QKMASTPGVS
510 520 530 540 550
ATFFNALAKA NINIRAIAQG CSEFNITVVV KREDCIRALR AVHSRFYLSR
560 570 580 590 600
TTLAVGIIGP GLIGGTLLDQ IRDQAAVLKE EFKIDLRVIG ITGSSKMLMS
610 620 630 640 650
ESGIDLSRWR ELMKEEGEKA DMEKFTQYVK GNHFIPNSVM VDCTADADIA
660 670 680 690 700
SCYYDWLLRG IHVVTPNKKA NSGPLDQYLK IRDLQRKSYT HYFYEATVGA
710 720 730 740 750
GLPIISTLRG LLETGDKILR IEGIFSGTLS YLFNNFVGTR SFSEVVAEAK
760 770 780 790 800
QAGFTEPDPR DDLSGTDVAR KVTILARESG LKLDLEGLPV QNLVPKPLQA
810 820 830 840 850
CASAEEFMEK LPQFDEELSK QREEAEAAGE VLRYVGVVDA VEKKGTVELK
860 870 880 890 900
RYKKDHPFAQ LSGADNIIAF TTKRYKEQPL IVRGPGAGAQ VTAGGIFSDI
910
LRLAFYLGAP S
Length:911
Mass (Da):99,404
Last modified:May 1, 2000 - v1
Checksum:i95A663413B68585F
GO

Sequence cautioni

The sequence AAF24602.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAA50500.2 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti517 – 5171I → M in BAC43372. (PubMed:11910074)Curated
Sequence conflicti900 – 9001I → F in BAC43372. (PubMed:11910074)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiE86438.
S46497.
RefSeqiNP_174408.1. NM_102861.3.
UniGeneiAt.48251.
At.71214.

Genome annotation databases

EnsemblPlantsiAT1G31230.1; AT1G31230.1; AT1G31230.
GeneIDi840011.
KEGGiath:AT1G31230.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiE86438.
S46497.
RefSeqiNP_174408.1. NM_102861.3.
UniGeneiAt.48251.
At.71214.

3D structure databases

ProteinModelPortaliQ9SA18.
SMRiQ9SA18. Positions 86-546, 549-904.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi25246. 1 interaction.
IntActiQ9SA18. 1 interaction.
MINTiMINT-8067838.

Proteomic databases

PaxDbiQ9SA18.
PRIDEiQ9SA18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G31230.1; AT1G31230.1; AT1G31230.
GeneIDi840011.
KEGGiath:AT1G31230.

Organism-specific databases

TAIRiAT1G31230.

Phylogenomic databases

eggNOGiCOG0527.
HOGENOMiHOG000271593.
InParanoidiQ9SA18.
KOiK12524.
OMAiPIEMRHD.
PhylomeDBiQ9SA18.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00015.
UPA00050; UER00063.
UPA00050; UER00461.
UPA00051; UER00462.
UPA00051; UER00465.
SABIO-RKQ9SA18.

Gene expression databases

GenevestigatoriQ9SA18.

Family and domain databases

Gene3Di3.40.1160.10. 2 hits.
3.40.50.720. 1 hit.
InterProiIPR002912. 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]
PfamiPF00696. AA_kinase. 1 hit.
PF01842. ACT. 2 hits.
PF00742. Homoserine_dh. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000727. ThrA. 1 hit.
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00657. asp_kinases. 1 hit.
PROSITEiPS51671. ACT. 2 hits.
PS00324. ASPARTOKINASE. 1 hit.
PS01042. HOMOSER_DHGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiAKH1_ARATH
AccessioniPrimary (citable) accession number: Q9SA18
Secondary accession number(s): Q8GWK9, Q9SHF9, Q9SW59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: May 1, 2000
Last modified: January 7, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.