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 25-NOV-2008, entry version 54. DE RecName: Full=Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic; DE Short=AK-HSDH 1; DE Short=AK-HD 1; DE AltName: Full=Beta-aspartyl phosphate homoserine 1; DE Includes: DE RecName: Full=Aspartokinase; DE EC=2.7.2.4; DE Includes: DE RecName: Full=Homoserine dehydrogenase; DE EC=1.1.1.3; DE Flags: Precursor; GN Name=AKHSDH1; Synonyms=AK-HSDH I; OrderedLocusNames=At1g31230; GN ORFNames=F28K20.19, T19E23.1; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA 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., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [2] 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 RT dehydrogenase from Arabidopsis thaliana."; RL Protein Expr. Purif. 24:105-110(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21932900; 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., RA Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., RA Shibata K., Shinagawa A., Shinozaki K.; RT "Functional annotation of a full-length Arabidopsis cDNA collection."; RL Science 296:141-145(2002). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-573. RC STRAIN=cv. Columbia; RX MEDLINE=94264241; 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 RT gene from Arabidopsis thaliana."; RL Plant Mol. Biol. 24:835-851(1994). RN [5] RP FUNCTION, ENZYME 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 RT thaliana aspartate kinase-homoserine dehydrogenase isoforms. RT Physiological context sets the specificity."; RL J. Biol. Chem. 280:41178-41183(2005). CC -!- CATALYTIC ACTIVITY: L-homoserine + NAD(P)(+) = L-aspartate 4- CC semialdehyde + NAD(P)H. CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L- CC aspartate. CC -!- ENZYME REGULATION: Inhibition of aspartate kinase activity by CC threonine and leucine and 3-fold activation by cysteine, CC isoleucine, valine, serine and alanine at 2.5 mM. Partial CC inhibition of homoserine dehydrogenase activity by threonine and CC cysteine (14% of activity remaining at saturation with either CC amino acid). No synergy between the effectors for both activation CC or inhibition. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=2.6 mM for aspartate for the aspartokinase activity (at pH CC 8.0, in the presence of 150 mM KCl, 20 mM MgCl(2), 200 uM NADPH CC and 20 mM ATP); CC KM=2.3 mM for aspartate for the aspartokinase activity (at pH CC 8.0, in the presence of 150 mM KCl, 20 mM MgCl(2), 200 uM NADPH, CC 20 mM ATP and a saturating concentration of alanine); CC KM=6.5 mM for ATP for the aspartokinase activity (at pH 8.0, in CC the presence of 150 mM KCl, 20 mM MgCl(2), 200 uM NADPH and 50 CC mM aspartate); CC KM=0.48 mM for ATP for the aspartokinase activity (at pH 8.0, in CC the presence of 150 mM KCl, 20 mM MgCl(2), 200 uM NADPH, 50 mM CC aspartate and a saturating concentration of alanine); CC KM=290 uM for aspartate semialdehyde for the forward reaction of CC the homoserine dehydrogenase activity (at pH 8.0, in the CC presence of 150 mM KCl and 200 uM NADPH); CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; tetrahydrodipicolinate from L-aspartate: step 1/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 1/3. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 3/3. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 1/5. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 3/5. CC -!- SUBUNIT: Homo- or heterodimer (Potential). CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC aspartokinase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the homoserine CC dehydrogenase family. CC -!- SIMILARITY: Contains 2 ACT domains. CC -!- SEQUENCE CAUTION: CC Sequence=AAF24602.1; Type=Erroneous gene model prediction; CC Sequence=CAA50500.2; Type=Erroneous gene model prediction; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC004793; AAD21689.1; -; Genomic_DNA. DR EMBL; AC007654; AAF24602.1; ALT_SEQ; 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; -. DR UniGene; At.71214; -. DR HSSP; P31116; 1EBF. DR ProMEX; Q9SA18; -. DR GeneID; 840011; -. DR GenomeReviews; CT485782_GR; AT1G31230. DR KEGG; ath:AT1G31230; -. DR NMPDR; fig|3702.1.peg.3465; -. DR TAIR; At1g31230; -. DR GermOnline; AT1G31230; Arabidopsis thaliana. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW. DR GO; GO:0010319; C:stromule; IDA:TAIR. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004072; F:aspartate kinase activity; IEA:InterPro. DR GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR002912; ACT_bd. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR005106; Asp/hSer_DHase_NAD-bd. DR InterPro; IPR001341; Asp_kin_reg. DR InterPro; IPR011147; bifunc_aspartokin/hSer_DHase. DR InterPro; IPR001342; hSer_DHase_cat. DR InterPro; IPR016040; NAD(P)-bd. DR Gene3D; G3DSA:3.40.1160.10; Aa_kinase; 1. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF01842; ACT; 2. DR Pfam; PF00742; Homoserine_dh; 1. DR Pfam; PF03447; NAD_binding_3; 1. DR PIRSF; PIRSF000727; ThrA; 1. DR TIGRFAMs; TIGR00657; asp_kinases; 1. DR PROSITE; PS00324; ASPARTOKINASE; 1. DR PROSITE; PS01042; HOMOSER_DHGENASE; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Chloroplast; Complete proteome; Kinase; KW Methionine biosynthesis; Multifunctional enzyme; NADP; Oxidoreductase; KW Plastid; Repeat; Transferase; Transit peptide. FT TRANSIT 1 82 Chloroplast (Potential). FT CHAIN 83 911 Bifunctional aspartokinase/homoserine FT dehydrogenase 1, chloroplastic. FT /FTId=PRO_0000245844. FT DOMAIN 403 471 ACT 1. FT DOMAIN 487 554 ACT 2. FT NP_BIND 559 564 NADP (Potential). FT REGION 83 331 Aspartokinase (By similarity). FT REGION 332 557 Interface (By similarity). FT REGION 558 911 Homoserine dehydrogenase (By similarity). FT CONFLICT 517 517 I -> M (in Ref. 3; BAC43372). FT CONFLICT 900 900 I -> F (in Ref. 3; BAC43372). 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 //