AKH2_ARATH
ID AKH2_ARATH Reviewed; 916 AA.
AC O81852; Q3E9Y8;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic;
DE Short=AK-HD 2;
DE Short=AK-HSDH 2;
DE AltName: Full=Beta-aspartyl phosphate homoserine 2;
DE Includes:
DE RecName: Full=Aspartokinase;
DE EC=2.7.2.4 {ECO:0000269|PubMed:16216875};
DE AltName: Full=Aspartate kinase {ECO:0000303|PubMed:16216875};
DE Includes:
DE RecName: Full=Homoserine dehydrogenase {ECO:0000303|PubMed:16216875};
DE EC=1.1.1.3 {ECO:0000269|PubMed:16216875};
DE Flags: Precursor;
GN Name=AKHSDH2; Synonyms=AK-HSDH II; OrderedLocusNames=At4g19710;
GN ORFNames=T16H5.70;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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] (ISOFORM 1), BIOPHYSICOCHEMICAL PROPERTIES,
RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP ACTIVITY REGULATION, MUTAGENESIS OF ILE-441; GLN-443; ILE-522 AND GLN-524,
RP AND CATALYTIC ACTIVITY.
RX PubMed=12435751; DOI=10.1074/jbc.m207379200;
RA Paris S., Viemon C., Curien G., Dumas R.;
RT "Mechanism of control of Arabidopsis thaliana aspartate kinase-homoserine
RT dehydrogenase by threonine.";
RL J. Biol. Chem. 278:5361-5366(2003).
RN [6]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL 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 -!- 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:11812230, ECO:0000269|PubMed:16216875};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15762;
CC Evidence={ECO:0000269|PubMed:12435751};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15763;
CC Evidence={ECO:0000269|PubMed:11812230, ECO:0000269|PubMed:12435751,
CC 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 -!- 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:11812230, ECO:0000269|PubMed:16216875};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23777;
CC Evidence={ECO:0000269|PubMed:11812230, ECO:0000269|PubMed:12435751,
CC ECO:0000269|PubMed:16216875};
CC -!- ACTIVITY REGULATION: Threonine interaction with Gln-443 leads to
CC inhibition of aspartate kinase activity and facilitates the binding of
CC a second threonine on Gln-524, leading to a partial inhibition of
CC homoserine dehydrogenase activity (25% of activity remaining at
CC saturation with threonine). Homoserine dehydrogenase activity is also
CC partially inhibited by cysteine (15% of activity remaining at
CC saturation with cysteine). No synergy between threonine and cysteine
CC for the inhibition. 13-fold activation of aspartate kinase activity by
CC cysteine, isoleucine, valine, serine and alanine at 2.5 mM and 4-fold
CC activation by leucine at 2.5 mM, but no activation of homoserine
CC dehydrogenase activity. {ECO:0000269|PubMed:11812230,
CC ECO:0000269|PubMed:12435751, ECO:0000269|PubMed:16216875}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.6 mM for aspartate for the aspartokinase activity (in the
CC presence of 40 mM ATP) {ECO:0000269|PubMed:11812230,
CC ECO:0000269|PubMed:16216875};
CC KM=6.15 mM for aspartate for the aspartokinase activity (at pH 8.0,
CC in the presence of 200 uM NADPH and 20 mM ATP)
CC {ECO:0000269|PubMed:11812230, ECO:0000269|PubMed:16216875};
CC KM=1.5 mM for aspartate for the aspartokinase activity (at pH 8.0, in
CC the presence of 200 uM NADPH, 20 mM ATP and a saturating
CC concentration of alanine) {ECO:0000269|PubMed:11812230,
CC ECO:0000269|PubMed:16216875};
CC KM=26.4 mM for aspartate for the aspartokinase activity (in the
CC presence of 100 mM ATP and 0.5 mM threonine)
CC {ECO:0000269|PubMed:11812230, ECO:0000269|PubMed:16216875};
CC KM=5.5 mM for ATP for the aspartokinase activity (in the presence of
CC 50 mM aspartate) {ECO:0000269|PubMed:11812230,
CC ECO:0000269|PubMed:16216875};
CC KM=2.2 mM for ATP for the aspartokinase activity (at pH 8.0, in the
CC presence of 200 uM NADPH and 50 mM aspartate)
CC {ECO:0000269|PubMed:11812230, ECO:0000269|PubMed:16216875};
CC KM=0.42 mM for ATP for the aspartokinase activity (at pH 8.0, in the
CC presence of 200 uM NADPH, 50 mM aspartate and a saturating
CC concentration of alanine) {ECO:0000269|PubMed:11812230,
CC ECO:0000269|PubMed:16216875};
CC KM=5.2 mM for homoserine for the reverse reaction of the homoserine
CC dehydrogenase activity (in the presence of 1 mM NADP)
CC {ECO:0000269|PubMed:11812230, ECO:0000269|PubMed:16216875};
CC KM=1.4 mM for aspartate semialdehyde for the forward reaction of the
CC homoserine dehydrogenase activity (in the presence of NADPH)
CC {ECO:0000269|PubMed:11812230, ECO:0000269|PubMed:16216875};
CC KM=311 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:11812230,
CC ECO:0000269|PubMed:16216875};
CC KM=24.5 mM for homoserine for the reverse reaction of the homoserine
CC dehydrogenase activity (in the presence of 1 mM NADP and 60 mM
CC threonine) {ECO:0000269|PubMed:11812230,
CC ECO:0000269|PubMed:16216875};
CC KM=166.1 uM for NADP for the reverse reaction of the homoserine
CC dehydrogenase activity (in the presence of 50 mM homoserine)
CC {ECO:0000269|PubMed:11812230, ECO:0000269|PubMed:16216875};
CC KM=676.1 uM for NADP for the reverse reaction of the homoserine
CC dehydrogenase activity (in the presence of 100 mM homoserine and 60
CC mM threonine) {ECO:0000269|PubMed:11812230,
CC ECO:0000269|PubMed:16216875};
CC Vmax=5.4 umol/min/mg enzyme toward aspartylhydroxamate for the
CC aspartokinase activity {ECO:0000269|PubMed:11812230,
CC ECO:0000269|PubMed:16216875};
CC Vmax=165 umol/min/mg enzyme toward aspartate semialdehyde for the
CC forward reaction of the homoserine dehydrogenase activity
CC {ECO:0000269|PubMed:11812230, ECO:0000269|PubMed:16216875};
CC Vmax=18.8 umol/min/mg enzyme toward NADPH for the reverse reaction of
CC the homoserine dehydrogenase activity {ECO:0000269|PubMed:11812230,
CC 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 -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 1/3.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 3/3.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 1/5.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 3/5.
CC -!- SUBUNIT: Homo- or heterodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O81852-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O81852-2; Sequence=VSP_019798;
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}.
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DR EMBL; AL024486; CAA19688.1; -; Genomic_DNA.
DR EMBL; AL161551; CAB78973.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84219.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84220.1; -; Genomic_DNA.
DR EMBL; BX827863; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T04752; T04752.
DR RefSeq; NP_193706.2; NM_118091.3. [O81852-2]
DR RefSeq; NP_974576.1; NM_202847.3. [O81852-1]
DR AlphaFoldDB; O81852; -.
DR SMR; O81852; -.
DR BioGRID; 13008; 1.
DR STRING; 3702.AT4G19710.2; -.
DR iPTMnet; O81852; -.
DR PaxDb; O81852; -.
DR PRIDE; O81852; -.
DR ProteomicsDB; 245073; -. [O81852-1]
DR EnsemblPlants; AT4G19710.1; AT4G19710.1; AT4G19710. [O81852-2]
DR EnsemblPlants; AT4G19710.2; AT4G19710.2; AT4G19710. [O81852-1]
DR GeneID; 827715; -.
DR Gramene; AT4G19710.1; AT4G19710.1; AT4G19710. [O81852-2]
DR Gramene; AT4G19710.2; AT4G19710.2; AT4G19710. [O81852-1]
DR KEGG; ath:AT4G19710; -.
DR Araport; AT4G19710; -.
DR TAIR; locus:2133995; AT4G19710.
DR eggNOG; ENOG502QQBK; Eukaryota.
DR HOGENOM; CLU_009116_7_1_1; -.
DR InParanoid; O81852; -.
DR OMA; CNKIACS; -.
DR PhylomeDB; O81852; -.
DR SABIO-RK; O81852; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR UniPathway; UPA00051; UER00465.
DR PRO; PR:O81852; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O81852; baseline and differential.
DR Genevisible; O81852; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; 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 Alternative splicing; Amino-acid biosynthesis; ATP-binding; Chloroplast;
KW Kinase; Methionine biosynthesis; Multifunctional enzyme; NADP;
KW Nucleotide-binding; Oxidoreductase; Plastid; Reference proteome; Repeat;
KW Transferase; Transit peptide.
FT TRANSIT 1..87
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 88..916
FT /note="Bifunctional aspartokinase/homoserine dehydrogenase
FT 2, chloroplastic"
FT /id="PRO_0000245845"
FT DOMAIN 412..487
FT /note="ACT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT DOMAIN 493..570
FT /note="ACT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT REGION 88..336
FT /note="Aspartokinase"
FT /evidence="ECO:0000250"
FT REGION 337..562
FT /note="Interface"
FT /evidence="ECO:0000250"
FT REGION 563..916
FT /note="Homoserine dehydrogenase"
FT /evidence="ECO:0000250"
FT BINDING 564..569
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT VAR_SEQ 837..916
FT /note="LRYVGVVDAVNQKGTVELRRYKKEHPFAQLAGSDNIIAFTTTRYKDHPLIVR
FT GPGAGAQVTAGGIFSDILRLASYLGAPS -> RLFTTNVFPFDQCDHILTIYICM (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_019798"
FT MUTAGEN 441
FT /note="I->A: Loss of threonine sensitivity for the
FT aspartokinase activity and decreased inhibition of
FT homoserine dehydrogenase activity by threonine."
FT /evidence="ECO:0000269|PubMed:12435751"
FT MUTAGEN 443
FT /note="Q->A: Loss of threonine sensitivity for the
FT aspartokinase activity and decreased inhibition of
FT homoserine dehydrogenase activity by threonine."
FT /evidence="ECO:0000269|PubMed:12435751"
FT MUTAGEN 522
FT /note="I->A: No effect on the inhibition of aspartokinase
FT activity by threonine, but decreased inhibition of
FT homoserine dehydrogenase activity by threonine."
FT /evidence="ECO:0000269|PubMed:12435751"
FT MUTAGEN 524
FT /note="Q->A: No effect on the inhibition of aspartokinase
FT activity by threonine, but decreased inhibition of
FT homoserine dehydrogenase activity by threonine."
FT /evidence="ECO:0000269|PubMed:12435751"
SQ SEQUENCE 916 AA; 100250 MW; 7ECD984DAFC97C4F CRC64;
MATLKPSFTV SPPNSNPIRF GSFPPQCFLR VPKPRRLILP RFRKTTGGGG GLIRCELPDF
HLSATATTVS GVSTVNLVDQ VQIPKGEMWS VHKFGGTCVG NSQRIRNVAE VIINDNSERK
LVVVSAMSKV TDMMYDLIRK AQSRDDSYLS ALEAVLEKHR LTARDLLDGD DLASFLSHLH
NDISNLKAML RAIYIAGHAS ESFSDFVAGH GELWSAQMLS YVVRKTGLEC KWMDTRDVLI
VNPTSSNQVD PDFGESEKRL DKWFSLNPSK IIIATGFIAS TPQNIPTTLK RDGSDFSAAI
MGALLRARQV TIWTDVDGVY SADPRKVNEA VILQTLSYQE AWEMSYFGAN VLHPRTIIPV
MRYNIPIVIR NIFNLSAPGT IICQPPEDDY DLKLTTPVKG FATIDNLALI NVEGTGMAGV
PGTASDIFGC VKDVGANVIM ISQASSEHSV CFAVPEKEVN AVSEALRSRF SEALQAGRLS
QIEVIPNCSI LAAVGQKMAS TPGVSCTLFS ALAKANINVR AISQGCSEYN VTVVIKREDS
VKALRAVHSR FFLSRTTLAM GIVGPGLIGA TLLDQLRDQA AVLKQEFNID LRVLGITGSK
KMLLSDIGID LSRWRELLNE KGTEADLDKF TQQVHGNHFI PNSVVVDCTA DSAIASRYYD
WLRKGIHVIT PNKKANSGPL DQYLKLRDLQ RKSYTHYFYE ATVGAGLPII STLRGLLETG
DKILRIEGIC SGTLSYLFNN FVGDRSFSEV VTEAKNAGFT EPDPRDDLSG TDVARKVIIL
ARESGLKLDL ADLPIRSLVP EPLKGCTSVE EFMEKLPQYD GDLAKERLDA ENSGEVLRYV
GVVDAVNQKG TVELRRYKKE HPFAQLAGSD NIIAFTTTRY KDHPLIVRGP GAGAQVTAGG
IFSDILRLAS YLGAPS
