[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; DOI=10.1111/j.1365-2958.1991.tb01893.x; PubMed=1956296 [NCBI, ExPASy, EBI, Israel, Japan] Kalinowski J., Cremer J., Bachmann B., Eggeling L., Sahm H., Puehler A.; "Genetic and biochemical analysis of the aspartokinase from Corynebacterium glutamicum."; Mol. Microbiol. 5:1197-1204(1991).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; Nakagawa S.; "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."; Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; DOI=10.1016/S0168-1656(03)00154-8; PubMed=12948626 [NCBI, ExPASy, EBI, Israel, Japan] Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.; "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."; J. Biotechnol. 104:5-25(2003).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; PubMed=8117072 [NCBI, ExPASy, EBI, Israel, Japan] Patek M., Krumbach K., Eggeling L., Sahm H.; "Leucine synthesis in Corynebacterium glutamicum: enzyme activities, structure of leuA, and effect of leuA inactivation on lysine synthesis."; Appl. Environ. Microbiol. 60:133-140(1994).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 158-421. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; DOI=10.1007/BF00262424; PubMed=1980002 [NCBI, ExPASy, EBI, Israel, Japan] Kalinowski J., Bachmann B., Thierbach G., Puehler A.; "Aspartokinase genes lysC alpha and lysC beta overlap and are adjacent to the aspartate beta-semialdehyde dehydrogenase gene asd in Corynebacterium glutamicum."; Mol. Gen. Genet. 224:317-324(1990).

Comments

CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-aspartate.
ENZYME REGULATION: Feedback inhibition by lysine and threonine.
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-threonine biosynthesis; L-threonine from L-aspartate: step 1/5 .
SUBUNIT: Tetramer consisting of two isoforms Alpha (catalytic) and two isoforms Beta (function not known).

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative initiation.

Name	Alpha
Synonyms	Aspartokinase subunit alpha
Isoform ID	P26512-1
This is the isoform sequence displayed in this entry.

Name	Beta
Synonyms	Aspartokinase subunit beta
Isoform ID	P26512-2
Features which should be applied to build the isoform sequence: VSP_018659, VSP_018660.

SIMILARITY: Belongs to the aspartokinase 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

X57226; CAA40502.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X57226; CAA40503.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000036; BAB97644.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX927148; CAF18822.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X70959; CAA50296.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I40723; I40723.
S15276; S15276.

RefSeq

NP_599504.1; -.
YP_224551.1; -.

3D structure databases

PDB

2DTJ; X-ray; 1.58 A; A/B=251-421.

[ExPASy / RCSB / EBI]

PDBsum

2DTJ; -.

ModBase

P26512.

Enzyme and pathway databases

BioCyc

CGLU196627-1:CG0306-MON; -.
MetaCyc:MON-6461; -.
MetaCyc:MON-6462; -.

Ontologies

GO:0016597;	Molecular function: amino acid binding (inferred from electronic annotation from InterPro).
GO:0004072;	Molecular function: aspartate kinase activity (inferred from electronic annotation from InterPro).
GO:0004349;	Molecular function: glutamate 5-kinase activity (inferred from electronic annotation from InterPro).
GO:0019877;	Biological process: diaminopimelate biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0006561;	Biological process: proline biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR002912; ACT_bd.
IPR001048; Asp/Glu/Uridylate_kinase.
IPR005260; Asp_kin_monofn.
IPR001341; Asp_kin_reg.
IPR001057; Glu_5kinase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.1160.10; Aa_kinase; 1.

Pfam

PF00696; AA_kinase; 1.
PF01842; ACT; 2.
Pfam graphical view of domain structure.

PRINTS

PR00474; GLU5KINASE.

TIGRFAMs

TIGR00656; asp_kin_monofn; 1.
TIGR00657; asp_kinases; 1.

PROSITE

PS00324; ASPARTOKINASE; 1.

Genome annotation databases

GeneID

1021294; -.
3345161; -.

GenomeReviews

BX927147_GR; cg0306.
BA000036_GR; Cgl0251.

KEGG

cgb:cg0306; -.
cgl:NCgl0247; -.

Phylogenomic databases

HOGENOM

P26512; -.

Genome annotation databases

CMR

P26512; Cgl0251.

Other

UniRef

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

Keywords

3D-structure; Alternative initiation; Amino-acid biosynthesis; Complete proteome; Diaminopimelate biosynthesis; Kinase; Lysine biosynthesis; Repeat; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 421`	`421`	`Aspartokinase.`	`PRO_0000002379`
`DOMAIN`	`266 339`	`74`	`ACT 1.`
`DOMAIN`	`348 413`	`66`	`ACT 2.`
`VAR_SEQ`	`1 249`		`Missing (in isoform Beta).`	`VSP_018659`
`VAR_SEQ`	`250 250`		`V -> M (in isoform Beta).`	`VSP_018660`
`MUTAGEN`	`301 301`		`S->Y: Feedback-resistant and enhanced expression of the asd gene.`
`CONFLICT`	`40 40`		`C -> V (in Ref. 1 and 4).`
`STRAND`	`254 261`	`8`
`STRAND`	`263 273`	`11`
`HELIX`	`278 288`	`11`
`STRAND`	`295 298`	`4`
`TURN`	`303 305`	`3`
`STRAND`	`307 315`	`9`
`HELIX`	`316 318`	`3`
`HELIX`	`319 327`	`9`
`TURN`	`328 334`	`7`
`STRAND`	`336 342`	`7`
`STRAND`	`344 352`	`9`
`HELIX`	`358 370`	`13`
`STRAND`	`377 381`	`5`
`STRAND`	`384 390`	`7`
`HELIX`	`391 393`	`3`
`HELIX`	`394 405`	`12`

Sequence information

Length: 421 AA [This is the length of the unprocessed precursor]

Molecular weight: 44755 Da [This is the MW of the unprocessed precursor]

CRC64: E36B4D0081DE0827 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALVVQKYGG SSLESAERIR NVAERIVATK KAGNDVVVVC SAMGDTTDEL LELAAAVNPV 

        70         80         90        100        110        120 
PPAREMDMLL TAGERISNAL VAMAIESLGA EAQSFTGSQA GVLTTERHGN ARIVDVTPGR 

       130        140        150        160        170        180 
VREALDEGKI CIVAGFQGVN KETRDVTTLG RGGSDTTAVA LAAALNADVC EIYSDVDGVY 

       190        200        210        220        230        240 
TADPRIVPNA QKLEKLSFEE MLELAAVGSK ILVLRSVEYA RAFNVPLRVR SSYSNDPGTL 

       250        260        270        280        290        300 
IAGSMEDIPV EEAVLTGVAT DKSEAKVTVL GISDKPGEAA KVFRALADAE INIDMVLQNV 

       310        320        330        340        350        360 
SSVEDGTTDI TFTCPRSDGR RAMEILKKLQ VQGNWTNVLY DDQVGKVSLV GAGMKSHPGV 

       370        380        390        400        410        420 
TAEFMEALRD VNVNIELIST SEIRISVLIR EDDLDAAARA LHEQFQLGGE DEAVVYAGTG 


R

P26512 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