[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=N13; PubMed=8100567 [NCBI, ExPASy, EBI, Israel, Japan] Follettie M.T., Peoples O.P., Agoropoulou C., Sinskey A.J.; "Gene structure and expression of the Corynebacterium flavum N13 ask-asd operon."; J. Bacteriol. 175:4096-4103(1993).

Comments

CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-aspartate.
ENZYME REGULATION: Low feedback inhibition by lysine and threonine. The decreased sensitivity of C.flavum, as compared to C.glutamicum, is probably due to the Asp-345-Gly sequence difference.
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 2 isoforms Alpha (catalytic) and 2 isoforms Beta (function not known) (By similarity).

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

Name	Alpha
Synonyms	Aspartokinase subunit alpha
Isoform ID	P41398-1
This is the isoform sequence displayed in this entry.

Name	Beta
Synonyms	Aspartokinase subunit beta
Isoform ID	P41398-2
Features which should be applied to build the isoform sequence: VSP_018657, VSP_018658.

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

L16848; AAA23293.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

P41398; 253-416.

ModBase

P41398.

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.

ProtoNet

P41398.

Other

UniRef

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

Keywords

Alternative initiation; Amino-acid biosynthesis; 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_0000002377`
`DOMAIN`	`266 339`	`74`	`ACT 1.`
`DOMAIN`	`348 413`	`66`	`ACT 2.`
`VAR_SEQ`	`1 249`		`Missing (in isoform Beta).`	`VSP_018657`
`VAR_SEQ`	`250 250`		`V -> M (in isoform Beta).`	`VSP_018658`
`MUTAGEN`	`345 345`		`D->G: Decreased sensitivity of AK activity to concerted feedback inhibition by lysine and threonine.`

Sequence information

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

Molecular weight: 44797 Da [This is the MW of the unprocessed precursor]

CRC64: 4B37B0B6597F665E [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 TFTCPRADGR RAMEILKKLQ VQGNWTNVLY DDQVDKVSLV GAGMKSHPGV 

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


R

P41398 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