NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tokyo 1998;
DOI=10.1038/35024074; PubMed=10993077 [NCBI, ExPASy, EBI, Israel, Japan]
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS.";
Nature 407:81-86(2000).

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: Homotetramer (By similarity).
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

BA000003; BAB12911.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_240025.1; -.

3D structure databases

HSSP

P31116; 1EBF. [HSSP ENTRY / PDB]

ModBase

P57290.

Enzyme and pathway databases

BioCyc

BSP107806:BU194-MON; -.

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; 1.
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

P57290.

Genome annotation databases

GeneID

1109637; -.

GenomeReviews

BA000003_GR; BU194.

KEGG

buc:BU194; -.

Phylogenomic databases

HOGENOM

P57290; -.

Genome annotation databases

CMR

P57290; BU194.

Other

ProtoNet

P57290.

UniRef

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

Keywords

Amino-acid biosynthesis; Complete proteome; Kinase; Multifunctional enzyme; NADP; Oxidoreductase; Threonine biosynthesis; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 816`	`816`	`Bifunctional aspartokinase/homoserine dehydrogenase.`	`PRO_0000066684`
`DOMAIN`	`398 468`	`71`	`ACT.`
`NP_BIND`	`472 479`	`8`	`NADP (Potential).`
`REGION`	`1 250`	`250`	`Aspartokinase (By similarity).`
`REGION`	`251 471`	`221`	`Interface (By similarity).`
`REGION`	`472 816`	`345`	`Homoserine dehydrogenase (By similarity).`

Sequence information

Length: 816 AA [This is the length of the unprocessed precursor]

Molecular weight: 91809 Da [This is the MW of the unprocessed precursor]

CRC64: CEACE5C565465884 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKLLKFGGTS LANAEKFLSV SSIIEENTQT DQIAVVLSAP AKITNYLVKI IENTIKNNQI 

        70         80         90        100        110        120 
LETVHLAENI FMQLINNFLN IQSNFPHKEI EKIIKKEFNE LKNIIQGILL LKQCPDNIRA 

       130        140        150        160        170        180 
IIISRGEILS VFIMKSILQS KNYNVTIINP VKNLVAIGDN YLDSTVDISE SKKNIQNMNI 

       190        200        210        220        230        240 
NQSNIILMAG FIAGNKDKKL VVLGRNGSDY SAAVLAACLD ANCCEIWTDV DGVFTSDPRK 

       250        260        270        280        290        300 
VPNARLLKSI SYQEAMELSY FGAKVLHPRT IEPIAQFKIP CLIKNTNNVK SIGTLICEQN 

       310        320        330        340        350        360 
CSEKDFLKGV THLDEIAMFN ISGPHIKDVG SVISRIFTMM SRGNIKILLI TQSSSENKIN 

       370        380        390        400        410        420 
FCVYEHDIYK ILYLFNKEFQ LELKDGLLNP FKIKKNLSIL SIVGSNIYKK HNIASKIFSV 

       430        440        450        460        470        480 
LGALKINVIA ISQGSSKHSI SLVIKKENIL KAVQHVHNTL FFNKKTIHMF LIGIGGIGST 

       490        500        510        520        530        540 
LLNQILKQKQ FLDKKNIEIK ICAIANSKKI LLLDNTNDLS NWKNDFKKST QKFNLELLNN 

       550        560        570        580        590        600 
LIKNNHFSNS VIVDCTSSQL LSEQYVNFID NNFHVVTSNK KANTSEWNYY KKIRKSVAQT 

       610        620        630        640        650        660 
GKKFLYETNV GAGLPVIETL QNLFKSGDNL ICFKGILSGS LSFIFGRLEE GILLSQATRE 

       670        680        690        700        710        720 
AKELGFTEPN PCDDLSGIDV ARKLLILARE SGYNIELKDI KIEPLLPNNF KIYEDTDKFL 

       730        740        750        760        770        780 
LKLKELDVYF SNKIKQALNV GNVLRFVATI EQKRQFFIKL EEVNINNPLY KVKNGENALA 

       790        800        810 
FYTNYYQPIP LVLRGYGAGN NVTASGVFSD LLRTLS

P57290 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