NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
DOI=10.1007/BF00014937; PubMed=8507831 [NCBI, ExPASy, EBI, Israel, Japan]
Weisemann J.M., Matthews B.F.;
"Identification and expression of a cDNA from Daucus carota encoding a bifunctional aspartokinase-homoserine dehydrogenase.";
Plant Mol. Biol. 22:301-312(1993).

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 .
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

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Cross-references

Sequence databases

EMBL

L11529; AAA16972.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S35160; S35160.

3D structure databases

HSSP

P31116; 1EBF. [HSSP ENTRY / PDB]

ModBase

P37142.

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.

Other

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

Keywords

Amino-acid biosynthesis; Chloroplast; Direct protein sequencing; 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 87`	`>87`	`Chloroplast.`
`CHAIN`	`88 921`	`834`	`Bifunctional aspartokinase/homoserine dehydrogenase, chloroplastic.`	`PRO_0000002391`
`DOMAIN`	`413 481`	`69`	`ACT 1.`
`DOMAIN`	`497 563`	`67`	`ACT 2.`
`NP_BIND`	`569 574`	`6`	`NADP (Potential).`
`REGION`	`88 339`	`252`	`Aspartokinase.`
`REGION`	`340 567`	`228`	`Interface.`
`REGION`	`568 921`	`354`	`Homoserine dehydrogenase.`
`NON_TER`	`1 1`

Sequence information

Length: 921 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 100226 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 9C89C392DA76A996 [This is a checksum on the sequence]

        10         20         30         40         50         60 
SLSSAISPSS YAAIAAAYSA RTPIFNKKKT AAVLSPLSLF HQSPSLSKTG IFLHRGRKES 

        70         80         90        100        110        120 
SSKFYIAASV TTAVPSLDDS VEKVHLPRGA MWSIHKFGGT CVGSSERIRN VAEIVVEDDS 

       130        140        150        160        170        180 
ERKLVVVSAM SKVTDMMYDL IYKAQSRDDS YESALDAVME KHKLTAFDLL DEDDLARFLT 

       190        200        210        220        230        240 
RLQHDVITLK AMLRAIYIAG HATESFSDFV VGHGELWSAQ LLSFVIRKNG GDCNWMDTRD 

       250        260        270        280        290        300 
VLVVNPAGSN QVDPDYLESE KRLEKWFSSN QCQTIVATGF IASTPQNIPT TLKRDGSDFS 

       310        320        330        340        350        360 
AAIMGALLRA GQVTIWTDVN GVYSADPRKV SEAVVLKTLS YQEAWEMSYF GANVLHPRTI 

       370        380        390        400        410        420 
NPVMRYDIPI VIRNIFNLSA PGTMICRESV GETEDGLKLE SHVKGFATID NLALINVEGT 

       430        440        450        460        470        480 
GMAGVPGTAT AIFGAVKDVG ANVIMISQAS SEHSICFAVP ESEVKAVAKA LEARFRQALD 

       490        500        510        520        530        540 
AGRLSQVANN PNCSILATVG QKMASTPGVS ATLFNALAKA NINVRAIAQG CTEYNITVVL 

       550        560        570        580        590        600 
SREDCVRALK AVHSRFYLSR TTIAVGIVGP GLIGATLLDQ LRDQAAILKE NSKIDLRVMG 

       610        620        630        640        650        660 
ITGSRTMLLS ETGIDLSRWR EVQKEKGQTA GLEKFVQHVR GNHFIPSTVI VDCTADSEVA 

       670        680        690        700        710        720 
SHYHDWLCRG IHVITPNKKA NSGPLDQYLK LRALQRRSYT HYFYEATVVA GLPIITTLQG 

       730        740        750        760        770        780 
LLETGDKILR IEGIFSGTLS YIFNNFKSTT PFSEVVSEAK AAGYTEPDPR DDLAGTDVAR 

       790        800        810        820        830        840 
KVIILARGSG LKLELSDIPV QSLVPEPLRG IASAEEFLLQ LPQFDSDMTR KREDAENAGE 

       850        860        870        880        890        900 
VLRYVGVVDA VNQKGVVELK RYKKEHPFAQ LSGSDNINAF TTERYNKQPP IIRGPGAGAE 

       910        920 
VTAGGVFSDI LRLASYLGAP S

P37142 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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