AKH2_MAIZE
ID AKH2_MAIZE Reviewed; 917 AA.
AC P49080;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic;
DE Short=AK-HD 2;
DE Short=AK-HSDH 2;
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=AKHSDH2;
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; L33913; AAA74361.1; -; mRNA.
DR PIR; T02954; T02954.
DR RefSeq; NP_001105691.1; NM_001112221.1.
DR RefSeq; XP_008668651.1; XM_008670429.1.
DR AlphaFoldDB; P49080; -.
DR SMR; P49080; -.
DR STRING; 4577.GRMZM2G104546_P02; -.
DR PaxDb; P49080; -.
DR PRIDE; P49080; -.
DR GeneID; 542708; -.
DR MaizeGDB; 66609; -.
DR eggNOG; ENOG502QQBK; Eukaryota.
DR HOGENOM; CLU_009116_7_1_1; -.
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; P49080; 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; 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; 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..89
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 90..917
FT /note="Bifunctional aspartokinase/homoserine dehydrogenase
FT 2, chloroplastic"
FT /id="PRO_0000002393"
FT DOMAIN 413..488
FT /note="ACT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT DOMAIN 494..571
FT /note="ACT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT REGION 90..338
FT /note="Aspartokinase"
FT REGION 339..563
FT /note="Interface"
FT REGION 564..917
FT /note="Homoserine dehydrogenase"
FT BINDING 565..570
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
SQ SEQUENCE 917 AA; 99583 MW; 69229EA13CAEA7E9 CRC64;
MQGLAVSCQL PPAAAAARWR PRASSSNREA VLQCWKYELS QDHYLGGPLR IGQSQGSLHR
HRSTNFLRPA AAAISVEQDE VNTYLPKGDM WSVHKFGGTC MGTPKRIQCV ANIVLGDSSE
RKLIIVSAMS KVTDMMYNLV QKAQSRDDSY AIALAEVFEK HMTAAKDLLD GEDLARFLSQ
LHSDVSNLRA MLRAIYIAGH ATESFSDFVV GHGELWSAQM LSYAIKKSGA PCSWMDTREV
LVVTPSGCNQ VDPDYLECEK RLQKWFSRQP AEIIVATGFI ASTAGNIPTT LKRDGSDFSA
AIVGSLVRAR QVTIWTDVDG VFSADPRKVS EAVILSTLSY QEAWEMSYFG ANVLHPRTII
PVMKDNIPIV IRNMFNLSAP GTMICKQPAN ENGDLDACVK SFATVDNLAL VNVEGTGMAG
VPGTASAIFS AVKDVGANVI MISQASSEHS VCFAVPEKEV AVVSAELHDR FREALAAGRL
SKVEVINGCS ILAAVGLRMA STPGVSAILF DALAKANINV RAIAQGCSEY NITVVLKQQD
CVRALRAAHS RFFLSKTTLA VGIIGPGLIG GALLNQLKNQ TAVLKENMNI DLRVIGITGS
STMLLSDTGI DLTQWKQLLQ KEAEPADIGS FVHHLSDNHV FPNKVLVDCT ADTSVASHYY
DWLKKGIHVI TPNKKANSGP LDQYLKLRTM QRASYTHYFY EATVGAGLPI ISTLRGLLET
GDKILRIEGI FSGTLSYIFN NFEGTRAFSD VVAEAREAGY TEPDPRDDLS GTDVARKVVV
LARESGLRLE LSDIPVKSLV PETLASCSSA DEFMQKLPSF DEDWARQRSD AEAAGEVLRY
VGALDAVNRS GQVELRRYRR DHPFAQLSGS DNIIAFTTSR YKEQPLIVRG PGAGAEVTAG
GVFCDILRLA SYLGAPS
