AKH1_ARATH
ID AKH1_ARATH Reviewed; 911 AA.
AC Q9SA18; Q8GWK9; Q9SHF9; Q9SW59;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic {ECO:0000305};
DE Short=AK-HD 1 {ECO:0000305};
DE Short=AK-HSDH 1 {ECO:0000303|PubMed:16216875};
DE AltName: Full=Beta-aspartyl phosphate homoserine 1 {ECO:0000305};
DE Includes:
DE RecName: Full=Aspartokinase {ECO:0000305};
DE EC=2.7.2.4 {ECO:0000269|PubMed:16216875};
DE Includes:
DE RecName: Full=Homoserine dehydrogenase {ECO:0000305};
DE EC=1.1.1.3 {ECO:0000269|PubMed:16216875};
DE Flags: Precursor;
GN Name=AKHSDH1 {ECO:0000305};
GN Synonyms=AK-HSDH I {ECO:0000303|PubMed:16216875};
GN OrderedLocusNames=At1g31230 {ECO:0000312|Araport:AT1G31230};
GN ORFNames=F28K20.19 {ECO:0000312|EMBL:AAD21689.1},
GN T19E23.1 {ECO:0000312|EMBL:AAF24602.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11812230; DOI=10.1006/prep.2001.1539;
RA Paris S., Wessel P.M., Dumas R.;
RT "Overproduction, purification, and characterization of recombinant
RT bifunctional threonine-sensitive aspartate kinase-homoserine dehydrogenase
RT from Arabidopsis thaliana.";
RL Protein Expr. Purif. 24:105-110(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-573.
RC STRAIN=cv. Columbia;
RX PubMed=8204822; DOI=10.1007/bf00014439;
RA Ghislain M., Frankard V., Vandenbossche D., Matthews B., Jacobs M.;
RT "Molecular analysis of the aspartate kinase-homoserine dehydrogenase gene
RT from Arabidopsis thaliana.";
RL Plant Mol. Biol. 24:835-851(1994).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=16216875; DOI=10.1074/jbc.m509324200;
RA Curien G., Ravanel S., Robert M., Dumas R.;
RT "Identification of six novel allosteric effectors of Arabidopsis thaliana
RT aspartate kinase-homoserine dehydrogenase isoforms. Physiological context
RT sets the specificity.";
RL J. Biol. Chem. 280:41178-41183(2005).
CC -!- FUNCTION: Bifunctional aspartate kinase and homoserine dehydrogenase
CC that catalyzes the first and the third steps toward the synthesis of
CC the essential amino acids threonine, isoleucine, and methionine.
CC {ECO:0000305|PubMed:16216875}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde +
CC NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC Evidence={ECO:0000269|PubMed:16216875};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15762;
CC Evidence={ECO:0000269|PubMed:16216875};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde +
CC NADH; Xref=Rhea:RHEA:15757, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC Evidence={ECO:0000269|PubMed:16216875};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15758;
CC Evidence={ECO:0000269|PubMed:16216875};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP;
CC Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4;
CC Evidence={ECO:0000269|PubMed:16216875};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23777;
CC Evidence={ECO:0000269|PubMed:16216875};
CC -!- ACTIVITY REGULATION: Inhibition of aspartate kinase activity by
CC threonine and leucine and 3-fold activation by cysteine, isoleucine,
CC valine, serine and alanine at 2.5 mM. Partial inhibition of homoserine
CC dehydrogenase activity by threonine and cysteine (14% of activity
CC remaining at saturation with either amino acid). No synergy between the
CC effectors for both activation or inhibition.
CC {ECO:0000269|PubMed:16216875}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.6 mM for aspartate for the aspartokinase activity (at pH 8.0, in
CC the presence of 150 mM KCl, 20 mM MgCl(2), 200 uM NADPH and 20 mM
CC ATP) {ECO:0000269|PubMed:16216875};
CC KM=2.3 mM for aspartate for the aspartokinase activity (at pH 8.0, in
CC the presence of 150 mM KCl, 20 mM MgCl(2), 200 uM NADPH, 20 mM ATP
CC and a saturating concentration of alanine)
CC {ECO:0000269|PubMed:16216875};
CC KM=6.5 mM for ATP for the aspartokinase activity (at pH 8.0, in the
CC presence of 150 mM KCl, 20 mM MgCl(2), 200 uM NADPH and 50 mM
CC aspartate) {ECO:0000269|PubMed:16216875};
CC KM=0.48 mM for ATP for the aspartokinase activity (at pH 8.0, in the
CC presence of 150 mM KCl, 20 mM MgCl(2), 200 uM NADPH, 50 mM aspartate
CC and a saturating concentration of alanine)
CC {ECO:0000269|PubMed:16216875};
CC KM=290 uM for aspartate semialdehyde for the forward reaction of the
CC homoserine dehydrogenase activity (at pH 8.0, in the presence of 150
CC mM KCl and 200 uM NADPH) {ECO:0000269|PubMed:16216875};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC {ECO:0000305|PubMed:16216875}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 1/3.
CC {ECO:0000305|PubMed:16216875}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 3/3.
CC {ECO:0000305|PubMed:16216875}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 1/5. {ECO:0000305|PubMed:16216875}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 3/5. {ECO:0000305|PubMed:16216875}.
CC -!- SUBUNIT: Homo- or heterodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the aspartokinase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the homoserine
CC dehydrogenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF24602.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA50500.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004793; AAD21689.1; -; Genomic_DNA.
DR EMBL; AC007654; AAF24602.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31330.1; -; Genomic_DNA.
DR EMBL; AK118779; BAC43372.1; -; mRNA.
DR EMBL; X71364; CAA50500.2; ALT_SEQ; Genomic_DNA.
DR PIR; E86438; E86438.
DR PIR; S46497; S46497.
DR RefSeq; NP_174408.1; NM_102861.3.
DR AlphaFoldDB; Q9SA18; -.
DR SMR; Q9SA18; -.
DR BioGRID; 25246; 3.
DR IntAct; Q9SA18; 1.
DR STRING; 3702.AT1G31230.1; -.
DR iPTMnet; Q9SA18; -.
DR PaxDb; Q9SA18; -.
DR PRIDE; Q9SA18; -.
DR ProteomicsDB; 244808; -.
DR EnsemblPlants; AT1G31230.1; AT1G31230.1; AT1G31230.
DR GeneID; 840011; -.
DR Gramene; AT1G31230.1; AT1G31230.1; AT1G31230.
DR KEGG; ath:AT1G31230; -.
DR Araport; AT1G31230; -.
DR TAIR; locus:2029564; AT1G31230.
DR eggNOG; ENOG502QQBK; Eukaryota.
DR HOGENOM; CLU_009116_7_1_1; -.
DR InParanoid; Q9SA18; -.
DR OMA; LCYRTPE; -.
DR OrthoDB; 113181at2759; -.
DR PhylomeDB; Q9SA18; -.
DR BRENDA; 2.7.2.4; 399.
DR SABIO-RK; Q9SA18; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR UniPathway; UPA00051; UER00465.
DR PRO; PR:Q9SA18; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SA18; baseline and differential.
DR Genevisible; Q9SA18; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0004072; F:aspartate kinase activity; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004412; F:homoserine dehydrogenase activity; IDA:TAIR.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0009067; P:aspartate family amino acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0009090; P:homoserine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04257; AAK_AK-HSDH; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR041743; AK-HSDH_N.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR InterPro; IPR001341; Asp_kinase.
DR InterPro; IPR018042; Aspartate_kinase_CS.
DR InterPro; IPR011147; Bifunc_aspartokin/hSer_DH.
DR InterPro; IPR027795; CASTOR_ACT_dom.
DR InterPro; IPR001342; HDH_cat.
DR InterPro; IPR019811; HDH_CS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43070; PTHR43070; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF13840; ACT_7; 1.
DR Pfam; PF00742; Homoserine_dh; 1.
DR Pfam; PF03447; NAD_binding_3; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
DR SUPFAM; SSF55021; SSF55021; 2.
DR TIGRFAMs; TIGR00657; asp_kinases; 1.
DR PROSITE; PS51671; ACT; 2.
DR PROSITE; PS00324; ASPARTOKINASE; 1.
DR PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; ATP-binding; Chloroplast; Kinase;
KW Methionine biosynthesis; Multifunctional enzyme; NADP; Nucleotide-binding;
KW Oxidoreductase; Plastid; Reference proteome; Repeat; Transferase;
KW Transit peptide.
FT TRANSIT 1..82
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 83..911
FT /note="Bifunctional aspartokinase/homoserine dehydrogenase
FT 1, chloroplastic"
FT /id="PRO_0000245844"
FT DOMAIN 407..482
FT /note="ACT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT DOMAIN 488..565
FT /note="ACT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT REGION 83..331
FT /note="Aspartokinase"
FT /evidence="ECO:0000250"
FT REGION 332..557
FT /note="Interface"
FT /evidence="ECO:0000250"
FT REGION 558..911
FT /note="Homoserine dehydrogenase"
FT /evidence="ECO:0000250"
FT BINDING 559..564
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT CONFLICT 517
FT /note="I -> M (in Ref. 4; BAC43372)"
FT /evidence="ECO:0000305"
FT CONFLICT 900
FT /note="I -> F (in Ref. 4; BAC43372)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 911 AA; 99404 MW; 95A663413B68585F CRC64;
MPVVSLAKVV TSPAVAGDLA VRVPFIYGKR LVSNRVSFGK LRRRSCIGQC VRSELQSPRV
LGSVTDLALD NSVENGHLPK GDSWAVHKFG GTCVGNSERI KDVAAVVVKD DSERKLVVVS
AMSKVTDMMY DLIHRAESRD DSYLSALSGV LEKHRATAVD LLDGDELSSF LARLNDDINN
LKAMLRAIYI AGHATESFSD FVVGHGELWS AQMLAAVVRK SGLDCTWMDA RDVLVVIPTS
SNQVDPDFVE SEKRLEKWFT QNSAKIIIAT GFIASTPQNI PTTLKRDGSD FSAAIMSALF
RSHQLTIWTD VDGVYSADPR KVSEAVVLKT LSYQEAWEMS YFGANVLHPR TIIPVMKYDI
PIVIRNIFNL SAPGTMICRQ IDDEDGFKLD APVKGFATID NLALVNVEGT GMAGVPGTAS
AIFSAVKEVG ANVIMISQAS SEHSVCFAVP EKEVKAVSEA LNSRFRQALA GGRLSQIEII
PNCSILAAVG QKMASTPGVS ATFFNALAKA NINIRAIAQG CSEFNITVVV KREDCIRALR
AVHSRFYLSR TTLAVGIIGP GLIGGTLLDQ IRDQAAVLKE EFKIDLRVIG ITGSSKMLMS
ESGIDLSRWR ELMKEEGEKA DMEKFTQYVK GNHFIPNSVM VDCTADADIA SCYYDWLLRG
IHVVTPNKKA NSGPLDQYLK IRDLQRKSYT HYFYEATVGA GLPIISTLRG LLETGDKILR
IEGIFSGTLS YLFNNFVGTR SFSEVVAEAK QAGFTEPDPR DDLSGTDVAR KVTILARESG
LKLDLEGLPV QNLVPKPLQA CASAEEFMEK LPQFDEELSK QREEAEAAGE VLRYVGVVDA
VEKKGTVELK RYKKDHPFAQ LSGADNIIAF TTKRYKEQPL IVRGPGAGAQ VTAGGIFSDI
LRLAFYLGAP S
