NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Seedling leaf;
DOI=10.1104/pp.106.4.1303; PubMed=7846152 [NCBI, ExPASy, EBI, Israel, Japan]
Muehlbauer G.J., Somers D.A., Matthews B.F., Gengenbach B.G.;
"Molecular genetics of the maize (Zea mays L.) aspartate kinase-homoserine dehydrogenase gene family.";
Plant Physiol. 106:1303-1312(1994).

Comments

CATALYTIC ACTIVITY: L-homoserine + NAD(P)⁺ = L-aspartate 4-semialdehyde + NAD(P)H.
CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-aspartate.
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; tetrahydrodipicolinate from L-aspartate: step 1/4 .
PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3 .
PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3 .
PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5 .
PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 3/5 .
SUBUNIT: Homo- or heterodimer (Potential).
SUBCELLULAR LOCATION: Plastid, chloroplast.
SIMILARITY: In the N-terminal section; belongs to the aspartokinase family.
SIMILARITY: In the C-terminal section; belongs to the homoserine dehydrogenase family.
SIMILARITY: Contains 2 ACT domains.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L33913; AAA74361.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

T02954; T02954.

NP_001105691.1; -.

3D structure databases

HSSP

P31116; 1EBF. [HSSP ENTRY / PDB]

ModBase

P49080.

Organism-specific databases

Gramene

P49080; -.

MaizeGDB

66609; -.

Family and domain databases

InterPro

IPR002912; ACT_bd.
IPR001048; Asp/Glu/Uridylate_kinase.
IPR005106; Asp/hSer_DHase_NAD-bd.
IPR001341; Asp_kin_reg.
IPR011147; bifunc_aspartokin/hSer_DHase.
IPR001342; hSer_DHase_cat.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.1160.10; Aa_kinase; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF00696; AA_kinase; 1.
PF01842; ACT; 2.
PF00742; Homoserine_dh; 1.
PF03447; NAD_binding_3; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000727; ThrA; 1.

TIGRFAMs

TIGR00657; asp_kinases; 1.

PROSITE

PS00324; ASPARTOKINASE; 1.
PS01042; HOMOSER_DHGENASE; 1.

BLOCKS

P49080.

Genome annotation databases

GeneID

542708; -.

Other

ProtoNet

P49080.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Chloroplast; Kinase; Methionine biosynthesis; Multifunctional enzyme; NADP; Oxidoreductase; Plastid; Repeat; Transferase; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 89`	`89`	`Chloroplast (Potential).`
`CHAIN`	`90 917`	`828`	`Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic.`	`PRO_0000002393`
`DOMAIN`	`409 483`	`75`	`ACT 1.`
`DOMAIN`	`493 560`	`68`	`ACT 2.`
`NP_BIND`	`565 570`	`6`	`NADP (Potential).`
`REGION`	`90 338`	`249`	`Aspartokinase.`
`REGION`	`339 563`	`225`	`Interface.`
`REGION`	`564 917`	`354`	`Homoserine dehydrogenase.`

Sequence information

Length: 917 AA [This is the length of the unprocessed precursor]

Molecular weight: 99583 Da [This is the MW of the unprocessed precursor]

CRC64: 69229EA13CAEA7E9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQGLAVSCQL PPAAAAARWR PRASSSNREA VLQCWKYELS QDHYLGGPLR IGQSQGSLHR 

        70         80         90        100        110        120 
HRSTNFLRPA AAAISVEQDE VNTYLPKGDM WSVHKFGGTC MGTPKRIQCV ANIVLGDSSE 

       130        140        150        160        170        180 
RKLIIVSAMS KVTDMMYNLV QKAQSRDDSY AIALAEVFEK HMTAAKDLLD GEDLARFLSQ 

       190        200        210        220        230        240 
LHSDVSNLRA MLRAIYIAGH ATESFSDFVV GHGELWSAQM LSYAIKKSGA PCSWMDTREV 

       250        260        270        280        290        300 
LVVTPSGCNQ VDPDYLECEK RLQKWFSRQP AEIIVATGFI ASTAGNIPTT LKRDGSDFSA 

       310        320        330        340        350        360 
AIVGSLVRAR QVTIWTDVDG VFSADPRKVS EAVILSTLSY QEAWEMSYFG ANVLHPRTII 

       370        380        390        400        410        420 
PVMKDNIPIV IRNMFNLSAP GTMICKQPAN ENGDLDACVK SFATVDNLAL VNVEGTGMAG 

       430        440        450        460        470        480 
VPGTASAIFS AVKDVGANVI MISQASSEHS VCFAVPEKEV AVVSAELHDR FREALAAGRL 

       490        500        510        520        530        540 
SKVEVINGCS ILAAVGLRMA STPGVSAILF DALAKANINV RAIAQGCSEY NITVVLKQQD 

       550        560        570        580        590        600 
CVRALRAAHS RFFLSKTTLA VGIIGPGLIG GALLNQLKNQ TAVLKENMNI DLRVIGITGS 

       610        620        630        640        650        660 
STMLLSDTGI DLTQWKQLLQ KEAEPADIGS FVHHLSDNHV FPNKVLVDCT ADTSVASHYY 

       670        680        690        700        710        720 
DWLKKGIHVI TPNKKANSGP LDQYLKLRTM QRASYTHYFY EATVGAGLPI ISTLRGLLET 

       730        740        750        760        770        780 
GDKILRIEGI FSGTLSYIFN NFEGTRAFSD VVAEAREAGY TEPDPRDDLS GTDVARKVVV 

       790        800        810        820        830        840 
LARESGLRLE LSDIPVKSLV PETLASCSSA DEFMQKLPSF DEDWARQRSD AEAAGEVLRY 

       850        860        870        880        890        900 
VGALDAVNRS GQVELRRYRR DHPFAQLSGS DNIIAFTTSR YKEQPLIVRG PGAGAEVTAG 

       910 
GVFCDILRLA SYLGAPS

P49080 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools