ID   AKH1_MAIZE              Reviewed;         920 AA.
AC   P49079;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-NOV-2008, entry version 64.
DE   RecName: Full=Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic;
DE            Short=AK-HSDH 1;
DE            Short=AK-HD 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;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae;
OC   PACCAD clade; Panicoideae; Andropogoneae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seedling leaf;
RX   MEDLINE=95148730; PubMed=7846152; DOI=10.1104/pp.106.4.1303;
RA   Muehlbauer G.J., Somers D.A., Matthews B.F., Gengenbach B.G.;
RT   "Molecular genetics of the maize (Zea mays L.) aspartate kinase-
RT   homoserine dehydrogenase gene family.";
RL   Plant Physiol. 106:1303-1312(1994).
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   -!- 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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; L33912; AAA74360.1; -; mRNA.
DR   PIR; T02953; T02953.
DR   RefSeq; NP_001105325.1; -.
DR   UniGene; Zm.94547; -.
DR   HSSP; P31116; 1EBF.
DR   GeneID; 542249; -.
DR   Gramene; P49079; -.
DR   MaizeGDB; 66609; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
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; 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   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Chloroplast; Kinase; Methionine biosynthesis;
KW   Multifunctional enzyme; NADP; Oxidoreductase; Plastid; Repeat;
KW   Transferase; Transit peptide.
FT   TRANSIT       1     92       Chloroplast (Potential).
FT   CHAIN        93    920       Bifunctional aspartokinase/homoserine
FT                                dehydrogenase 1, chloroplastic.
FT                                /FTId=PRO_0000002392.
FT   DOMAIN      412    480       ACT 1.
FT   DOMAIN      496    563       ACT 2.
FT   NP_BIND     568    573       NADP (Potential).
FT   REGION       93    341       Aspartokinase.
FT   REGION      342    566       Interface.
FT   REGION      567    920       Homoserine dehydrogenase.
SQ   SEQUENCE   920 AA;  100336 MW;  08DCF444BE645529 CRC64;
     MRSLTVASRH PGAAFSTRRR PLLHPAAAGR DSTFQRCWRW EKTQDSSFGS SLRTSRLPRT
     VHGDILKNLL APTAGAVSVE QAEAIADLPK GDMWSVHKFG GTCMGTSERI HNVADIVLRD
     PSERKLVVVS AMSKVTDMMY NLVNKAQSRD DSYIAVLDEV FDKHMTTAKD LLAGEDLARF
     LSQLHADISN LKAMLRAIYI AGHATESFSD FVVGHGELWS AQMLSYAIQK SGTPCSWMDT
     REVLVVNPSG ANQVDPDYLE SEKRLEKWFS RCPAETIIAT GFIASTPENI PTTLKRDGSD
     FSAAIIGSLV KARQVTIWTD VDGVFSADPR KVSEAVILST LSYQEAWEMS YFGANVLHPR
     TIIPVMKYNI PIVIRNIFNT SAPGTMICQQ PANENGDLEA CVKAFATIDK LALVNVEGTG
     MAGVPGTANA IFGAVKDVGA NVIMISQASS EHSVCFAVPE KEVALVSAAL HARFREALAA
     GRLSKVEVIH NCSILATVGL RMASTPGVSA TLFDALAKAN INVRAIAQGC SEYNITIVLK
     QEDCVRALRA AHSRFFLSKT TLAVGIIGPG LIGRTLLNQL KDQAAVLKEN MNIDLRVMGI
     AGSRTMLLSD IGVDLTQWKE KLQTEAEPAN LDKFVHHLSE NHFFPNRVLV DCTADTSVAS
     HYYDWLKKGI HVITPNKKAN SGPLDRYLKL RTLQRASYTH YFYEATVGAG LPIISTLRGL
     LETGDKILRI EGIFSGTLSY IFNNFEGART FSDVVAEAKK AGYTEPDPRD DLSGTDVARK
     VIILARESGL GLELSDIPVR SLVPEALKSC TSADEYMQKL PSFDEDWARE RKNAEAAGEV
     LRYVGVVDVV SKKGQVELRA YKRDHPFAQL SGSDNIIAFT TSRYKDQPLI VRGPGAGAEV
     TAGGVFCDIL RLSSYLGAPS
//