[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-10. PubMed=6298218 [NCBI, ExPASy, EBI, Israel, Japan] Zakin M.M., Duchange N., Ferrara P., Cohen G.N.; "Nucleotide sequence of the metL gene of Escherichia coli. Its product, the bifunctional aspartokinase II-homoserine dehydrogenase II, and the bifunctional product of the thrA gene, aspartokinase I-homoserine dehydrogenase I, derive from a common ancestor."; J. Biol. Chem. 258:3028-3031(1983).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1093/nar/21.15.3391; PubMed=8346018 [NCBI, ExPASy, EBI, Israel, Japan] Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.; "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."; Nucleic Acids Res. 21:3391-3398(1993).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).

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.
MISCELLANEOUS: Aspartokinase I-homoserine dehydrogenase I and aspartokinase III also catalyze the same reaction(s).
SIMILARITY: In the N-terminal section; belongs to the aspartokinase family.
SIMILARITY: In the C-terminal section; belongs to the homoserine dehydrogenase family.

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

V00305; CAA23585.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L19201; AAB03072.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76922.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77370.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S40883; DEECK2.

RefSeq

AP_003869.1; -.
NP_418375.1; -.

3D structure databases

HSSP

P31116; 1EBF. [HSSP ENTRY / PDB]

ModBase

P00562.

Protein-protein interaction databases

IntAct

P00562; -.

Enzyme and pathway databases

BioCyc

EcoCyc:ASPKINIIHOMOSERDEHYDROGII-MON; -.
MetaCyc:ASPKINIIHOMOSERDEHYDROGII-MON; -.

Organism-specific databases

EchoBASE

EB0585; -.

EcoGene

EG10590; metL.

Family and domain databases

InterPro

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.
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

P00562.

Genome annotation databases

GeneID

948433; -.

GenomeReviews

U00096_GR; b3940.
AP009048_GR; JW3911.

KEGG

ecj:JW3911; -.
eco:b3940; -.

Phylogenomic databases

HOGENOM

P00562; -.

Genome annotation databases

CMR

P00562; b3940.

Other

ProtoNet

P00562.

UniRef

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

Keywords

Amino-acid biosynthesis; Complete proteome; Direct protein sequencing; Kinase; Methionine biosynthesis; Multifunctional enzyme; NADP; Oxidoreductase; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 810`	`809`	`Bifunctional aspartokinase/homoserine dehydrogenase 2.`	`PRO_0000066683`
`NP_BIND`	`464 471`	`8`	`NADP (Potential).`
`REGION`	`2 252`	`251`	`Aspartokinase.`
`REGION`	`253 463`	`211`	`Interface.`
`REGION`	`464 810`	`347`	`Homoserine dehydrogenase.`
`CONFLICT`	`56 56`		`Q -> R (in Ref. 1; CAA23585).`
`CONFLICT`	`59 59`		`N -> S (in Ref. 1; CAA23585).`
`CONFLICT`	`333 333`		`A -> G (in Ref. 1; CAA23585).`
`CONFLICT`	`674 674`		`M -> S (in Ref. 1; CAA23585).`
`CONFLICT`	`762 762`		`A -> R (in Ref. 1; CAA23585).`

Sequence information

Length: 810 AA [This is the length of the unprocessed precursor]

Molecular weight: 88888 Da [This is the MW of the unprocessed precursor]

CRC64: BD2515E3554F9B44 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSVIAQAGAK GRQLHKFGGS SLADVKCYLR VAGIMAEYSQ PDDMMVVSAA GSTTNQLINW 

        70         80         90        100        110        120 
LKLSQTDRLS AHQVQQTLRR YQCDLISGLL PAEEADSLIS AFVSDLERLA ALLDSGINDA 

       130        140        150        160        170        180 
VYAEVVGHGE VWSARLMSAV LNQQGLPAAW LDAREFLRAE RAAQPQVDEG LSYPLLQQLL 

       190        200        210        220        230        240 
VQHPGKRLVV TGFISRNNAG ETVLLGRNGS DYSATQIGAL AGVSRVTIWS DVAGVYSADP 

       250        260        270        280        290        300 
RKVKDACLLP LLRLDEASEL ARLAAPVLHA RTLQPVSGSE IDLQLRCSYT PDQGSTRIER 

       310        320        330        340        350        360 
VLASGTGARI VTSHDDVCLI EFQVPASQDF KLAHKEIDQI LKRAQVRPLA VGVHNDRQLL 

       370        380        390        400        410        420 
QFCYTSEVAD SALKILDEAG LPGELRLRQG LALVAMVGAG VTRNPLHCHR FWQQLKGQPV 

       430        440        450        460        470        480 
EFTWQSDDGI SLVAVLRTGP TESLIQGLHQ SVFRAEKRIG LVLFGKGNIG SRWLELFARE 

       490        500        510        520        530        540 
QSTLSARTGF EFVLAGVVDS RRSLLSYDGL DASRALAFFN DEAVEQDEES LFLWMRAHPY 

       550        560        570        580        590        600 
DDLVVLDVTA SQQLADQYLD FASHGFHVIS ANKLAGASDS NKYRQIHDAF EKTGRHWLYN 

       610        620        630        640        650        660 
ATVGAGLPIN HTVRDLIDSG DTILSISGIF SGTLSWLFLQ FDGSVPFTEL VDQAWQQGLT 

       670        680        690        700        710        720 
EPDPRDDLSG KDVMRKLVIL AREAGYNIEP DQVRVESLVP AHCEGGSIDH FFENGDELNE 

       730        740        750        760        770        780 
QMVQRLEAAR EMGLVLRYVA RFDANGKARV GVEAVREDHP LASLLPCDNV FAIESRWYRD 

       790        800        810 
NPLVIRGPGA GRDVTAGAIQ SDINRLAQLL

P00562 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