ID   AKH_DAUCA               Reviewed;         921 AA.
AC   P37142;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   04-NOV-2008, entry version 59.
DE   RecName: Full=Bifunctional aspartokinase/homoserine dehydrogenase, chloroplastic;
DE            Short=AK-HSDH;
DE            Short=AK-HD;
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; Fragment;
OS   Daucus carota (Carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae;
OC   Daucinae; Daucus.
OX   NCBI_TaxID=4039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=93283634; PubMed=8507831; DOI=10.1007/BF00014937;
RA   Weisemann J.M., Matthews B.F.;
RT   "Identification and expression of a cDNA from Daucus carota encoding a
RT   bifunctional aspartokinase-homoserine dehydrogenase.";
RL   Plant Mol. Biol. 22:301-312(1993).
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   -!- 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   -!- 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.
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DR   EMBL; L11529; AAA16972.1; -; mRNA.
DR   PIR; S35160; S35160.
DR   HSSP; P31116; 1EBF.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
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; 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   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; Direct protein sequencing;
KW   Kinase; Methionine biosynthesis; Multifunctional enzyme; NADP;
KW   Oxidoreductase; Plastid; Repeat; Transferase; Transit peptide.
FT   TRANSIT      <1     87       Chloroplast.
FT   CHAIN        88    921       Bifunctional aspartokinase/homoserine
FT                                dehydrogenase, chloroplastic.
FT                                /FTId=PRO_0000002391.
FT   DOMAIN      413    481       ACT 1.
FT   DOMAIN      497    563       ACT 2.
FT   NP_BIND     569    574       NADP (Potential).
FT   REGION       88    339       Aspartokinase.
FT   REGION      340    567       Interface.
FT   REGION      568    921       Homoserine dehydrogenase.
FT   NON_TER       1      1
SQ   SEQUENCE   921 AA;  100226 MW;  9C89C392DA76A996 CRC64;
     SLSSAISPSS YAAIAAAYSA RTPIFNKKKT AAVLSPLSLF HQSPSLSKTG IFLHRGRKES
     SSKFYIAASV TTAVPSLDDS VEKVHLPRGA MWSIHKFGGT CVGSSERIRN VAEIVVEDDS
     ERKLVVVSAM SKVTDMMYDL IYKAQSRDDS YESALDAVME KHKLTAFDLL DEDDLARFLT
     RLQHDVITLK AMLRAIYIAG HATESFSDFV VGHGELWSAQ LLSFVIRKNG GDCNWMDTRD
     VLVVNPAGSN QVDPDYLESE KRLEKWFSSN QCQTIVATGF IASTPQNIPT TLKRDGSDFS
     AAIMGALLRA GQVTIWTDVN GVYSADPRKV SEAVVLKTLS YQEAWEMSYF GANVLHPRTI
     NPVMRYDIPI VIRNIFNLSA PGTMICRESV GETEDGLKLE SHVKGFATID NLALINVEGT
     GMAGVPGTAT AIFGAVKDVG ANVIMISQAS SEHSICFAVP ESEVKAVAKA LEARFRQALD
     AGRLSQVANN PNCSILATVG QKMASTPGVS ATLFNALAKA NINVRAIAQG CTEYNITVVL
     SREDCVRALK AVHSRFYLSR TTIAVGIVGP GLIGATLLDQ LRDQAAILKE NSKIDLRVMG
     ITGSRTMLLS ETGIDLSRWR EVQKEKGQTA GLEKFVQHVR GNHFIPSTVI VDCTADSEVA
     SHYHDWLCRG IHVITPNKKA NSGPLDQYLK LRALQRRSYT HYFYEATVVA GLPIITTLQG
     LLETGDKILR IEGIFSGTLS YIFNNFKSTT PFSEVVSEAK AAGYTEPDPR DDLAGTDVAR
     KVIILARGSG LKLELSDIPV QSLVPEPLRG IASAEEFLLQ LPQFDSDMTR KREDAENAGE
     VLRYVGVVDA VNQKGVVELK RYKKEHPFAQ LSGSDNINAF TTERYNKQPP IIRGPGAGAE
     VTAGGVFSDI LRLASYLGAP S
//