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   03-AUG-2022, entry version 122.
DE   RecName: Full=Bifunctional aspartokinase/homoserine dehydrogenase, chloroplastic;
DE            Short=AK-HD;
DE            Short=AK-HSDH;
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 (Wild carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=4039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   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:
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   -!- 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   -!- 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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L11529; AAA16972.1; -; mRNA.
DR   PIR; S35160; S35160.
DR   AlphaFoldDB; P37142; -.
DR   SMR; P37142; -.
DR   PRIDE; P37142; -.
DR   SABIO-RK; P37142; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   UniPathway; UPA00051; UER00465.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
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;
KW   Direct protein sequencing; Kinase; Methionine biosynthesis;
KW   Multifunctional enzyme; NADP; Nucleotide-binding; Oxidoreductase; Plastid;
KW   Repeat; Transferase; Transit peptide.
FT   TRANSIT         <1..87
FT                   /note="Chloroplast"
FT   CHAIN           88..921
FT                   /note="Bifunctional aspartokinase/homoserine dehydrogenase,
FT                   chloroplastic"
FT                   /id="PRO_0000002391"
FT   DOMAIN          417..489
FT                   /note="ACT 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   DOMAIN          498..575
FT                   /note="ACT 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   REGION          88..339
FT                   /note="Aspartokinase"
FT   REGION          340..567
FT                   /note="Interface"
FT   REGION          568..921
FT                   /note="Homoserine dehydrogenase"
FT   BINDING         569..574
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255"
FT   NON_TER         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