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

L33912; AAA74360.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

T02953; T02953.

NP_001105325.1; -.

3D structure databases

HSSP

P31116; 1EBF. [HSSP ENTRY / PDB]

ModBase

P49079.

Organism-specific databases

Gramene

P49079; -.

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.
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.

TIGRFAMs

TIGR00657; asp_kinases; 1.

PROSITE

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

BLOCKS

P49079.

Genome annotation databases

GeneID

542249; -.

Other

ProtoNet

P49079.

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 92`	`92`	`Chloroplast (Potential).`
`CHAIN`	`93 920`	`828`	`Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic.`	`PRO_0000002392`
`DOMAIN`	`412 480`	`69`	`ACT 1.`
`DOMAIN`	`496 563`	`68`	`ACT 2.`
`NP_BIND`	`568 573`	`6`	`NADP (Potential).`
`REGION`	`93 341`	`249`	`Aspartokinase.`
`REGION`	`342 566`	`225`	`Interface.`
`REGION`	`567 920`	`354`	`Homoserine dehydrogenase.`

Sequence information

Length: 920 AA [This is the length of the unprocessed precursor]

Molecular weight: 100336 Da [This is the MW of the unprocessed precursor]

CRC64: 08DCF444BE645529 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRSLTVASRH PGAAFSTRRR PLLHPAAAGR DSTFQRCWRW EKTQDSSFGS SLRTSRLPRT 

        70         80         90        100        110        120 
VHGDILKNLL APTAGAVSVE QAEAIADLPK GDMWSVHKFG GTCMGTSERI HNVADIVLRD 

       130        140        150        160        170        180 
PSERKLVVVS AMSKVTDMMY NLVNKAQSRD DSYIAVLDEV FDKHMTTAKD LLAGEDLARF 

       190        200        210        220        230        240 
LSQLHADISN LKAMLRAIYI AGHATESFSD FVVGHGELWS AQMLSYAIQK SGTPCSWMDT 

       250        260        270        280        290        300 
REVLVVNPSG ANQVDPDYLE SEKRLEKWFS RCPAETIIAT GFIASTPENI PTTLKRDGSD 

       310        320        330        340        350        360 
FSAAIIGSLV KARQVTIWTD VDGVFSADPR KVSEAVILST LSYQEAWEMS YFGANVLHPR 

       370        380        390        400        410        420 
TIIPVMKYNI PIVIRNIFNT SAPGTMICQQ PANENGDLEA CVKAFATIDK LALVNVEGTG 

       430        440        450        460        470        480 
MAGVPGTANA IFGAVKDVGA NVIMISQASS EHSVCFAVPE KEVALVSAAL HARFREALAA 

       490        500        510        520        530        540 
GRLSKVEVIH NCSILATVGL RMASTPGVSA TLFDALAKAN INVRAIAQGC SEYNITIVLK 

       550        560        570        580        590        600 
QEDCVRALRA AHSRFFLSKT TLAVGIIGPG LIGRTLLNQL KDQAAVLKEN MNIDLRVMGI 

       610        620        630        640        650        660 
AGSRTMLLSD IGVDLTQWKE KLQTEAEPAN LDKFVHHLSE NHFFPNRVLV DCTADTSVAS 

       670        680        690        700        710        720 
HYYDWLKKGI HVITPNKKAN SGPLDRYLKL RTLQRASYTH YFYEATVGAG LPIISTLRGL 

       730        740        750        760        770        780 
LETGDKILRI EGIFSGTLSY IFNNFEGART FSDVVAEAKK AGYTEPDPRD DLSGTDVARK 

       790        800        810        820        830        840 
VIILARESGL GLELSDIPVR SLVPEALKSC TSADEYMQKL PSFDEDWARE RKNAEAAGEV 

       850        860        870        880        890        900 
LRYVGVVDVV SKKGQVELRA YKRDHPFAQL SGSDNIIAFT TSRYKDQPLI VRGPGAGAEV 

       910        920 
TAGGVFCDIL RLSSYLGAPS

P49079 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