Bifunctional aspartokinase/homoserine dehydrogenase, chloroplastic precursor - Daucus carota (Carrot)

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Reviewed, UniProtKB/Swiss-Prot P37142 (AKH_DAUCA)

Last modified June 16, 2009. Version 66. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names	Recommended name: Bifunctional aspartokinase/homoserine dehydrogenase, chloroplastic Short name=AK-HSDH Short name=AK-HD Including the following 2 domains: 1- Recommended name: Aspartokinase EC=2.7.2.4 2- Recommended name: Homoserine dehydrogenase EC=1.1.1.3
Organism	Daucus carota (Carrot)
Taxonomic identifier	4039 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › campanulids › Apiales › Apiaceae › Apioideae › Scandiceae › Daucinae › Daucus

Protein attributes

Sequence length	921 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	L-homoserine + NAD(P)⁺ = L-aspartate 4-semialdehyde + NAD(P)H. 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. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 3/5.
Subcellular location	Plastid › chloroplast.
Sequence similarities	In the N-terminal section; belongs to the aspartokinase family. In the C-terminal section; belongs to the homoserine dehydrogenase family. Contains 2 ACT domains.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis
Cellular component	Chloroplast Plastid
Domain	Repeat Transit peptide
Ligand	ATP-binding NADP Nucleotide-binding
Molecular function	Kinase Oxidoreductase Transferase
Technical term	Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW NADP or NADPH binding Inferred from electronic annotation. Source: InterPro amino acid binding Inferred from electronic annotation. Source: InterPro aspartate kinase activity Inferred from electronic annotation. Source: EC homoserine dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

›87

Chloroplast

Chain

834

Bifunctional aspartokinase/homoserine dehydrogenase, chloroplastic

PRO_0000002391

Regions

Domain

69

ACT 1

Domain

67

ACT 2

Nucleotide binding

6

NADP Potential

Region

252

Aspartokinase

Region

228

Interface

Region

354

Homoserine dehydrogenase

Experimental info

Non-terminal residue

1

Sequences

Sequence

Length

Mass (Da)

Tools

P37142-1 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 9C89C392DA76A996
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921

100,226

        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

References

[1]	"Identification and expression of a cDNA from Daucus carota encoding a bifunctional aspartokinase-homoserine dehydrogenase." Weisemann J.M., Matthews B.F. Plant Mol. Biol. 22:301-312(1993) [PubMed: 8507831] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.

Cross-references

Sequence databases
	L11529 mRNA. Translation: AAA16972.1.
PIR	S35160.
3D structure databases
HSSP	HSSP built from PDB template 1EBF based on UniProtKB P31116.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.3. 1081. 2.7.2.4. 1081.
Family and domain databases
InterPro	IPR002912. ACT_bd. IPR001048. Asp/Glu/Uridylate_kinase. IPR005106. Asp/hSer_DH_NAD-bd. IPR001341. Asp_kin_reg. IPR018042. Aspartate_kinase_CS. IPR001342. Homoserine_dehydrogenase_cat. IPR019811. Homoserine_dehydrogenase_CS. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.1160.10. Aa_kinase. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00696. AA_kinase. 1 hit. PF01842. ACT. 2 hits. PF00742. Homoserine_dh. 1 hit. PF03447. NAD_binding_3. 1 hit. [Graphical view]
TIGRFAMs	TIGR00657. asp_kinases. 1 hit.
PROSITE	PS00324. ASPARTOKINASE. 1 hit. PS01042. HOMOSER_DHGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AKH_DAUCA

Accession

Primary (citable) accession number: P37142

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents