AKH1_MAIZE
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 03-AUG-2022, entry version 141.
DE RecName: Full=Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic;
DE Short=AK-HD 1;
DE Short=AK-HSDH 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; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Seedling leaf;
RX 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-homoserine
RT dehydrogenase gene family.";
RL Plant Physiol. 106:1303-1312(1994).
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 -!- SUBUNIT: Homo- or heterodimer. {ECO:0000305}.
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}.
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DR EMBL; L33912; AAA74360.1; -; mRNA.
DR PIR; T02953; T02953.
DR RefSeq; NP_001105325.1; NM_001111855.2.
DR AlphaFoldDB; P49079; -.
DR SMR; P49079; -.
DR STRING; 4577.GRMZM2G365423_P01; -.
DR PaxDb; P49079; -.
DR PRIDE; P49079; -.
DR GeneID; 542249; -.
DR KEGG; zma:542249; -.
DR MaizeGDB; 66609; -.
DR eggNOG; ENOG502QQBK; Eukaryota.
DR OrthoDB; 113181at2759; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P49079; baseline and differential.
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; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Amino-acid biosynthesis; ATP-binding; Chloroplast; Kinase;
KW Methionine biosynthesis; Multifunctional enzyme; NADP; Nucleotide-binding;
KW Oxidoreductase; Plastid; Reference proteome; Repeat; Transferase;
KW Transit peptide.
FT TRANSIT 1..92
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 93..920
FT /note="Bifunctional aspartokinase/homoserine dehydrogenase
FT 1, chloroplastic"
FT /id="PRO_0000002392"
FT DOMAIN 416..491
FT /note="ACT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT DOMAIN 497..574
FT /note="ACT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..341
FT /note="Aspartokinase"
FT REGION 342..566
FT /note="Interface"
FT REGION 567..920
FT /note="Homoserine dehydrogenase"
FT BINDING 568..573
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
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
