NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 607 / DSM 43465 / mc(2)6 / NCTC 7017 / NRRL B-692;
PubMed=7910936 [NCBI, ExPASy, EBI, Israel, Japan]
Cirillo J.D., Weisbrod T.R., Pascopella L., Bloom B.R., Jacobs W.R. Jr.;
"Isolation and characterization of the aspartokinase and aspartate semialdehyde dehydrogenase operon from mycobacteria.";
Mol. Microbiol. 11:629-639(1994).

Comments

CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-aspartate.
ENZYME REGULATION: Feedback inhibition by lysine and threonine (By similarity).
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	P41403-1
This is the isoform sequence displayed in this entry.

Name	Beta
Synonyms	Aspartokinase subunit beta
Isoform ID	P41403-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_018662.

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

Z17372; CAA78984.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z17372; CAA78985.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S42422; S42422.

3D structure databases

ModBase

P41403.

Family and domain databases

InterPro

IPR002912; ACT_bd.
IPR001048; Asp/Glu/Uridylate_kinase.
IPR005260; Asp_kin_monofn.
IPR001341; Asp_kin_reg.
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.

TIGRFAMs

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

PROSITE

PS00324; ASPARTOKINASE; 1.

Other

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_0000002383`
`DOMAIN`	`266 341`	`76`	`ACT 1.`
`DOMAIN`	`348 413`	`66`	`ACT 2.`
`VAR_SEQ`	`1 249`		`Missing (in isoform Beta).`	`VSP_018662`

Sequence information

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

Molecular weight: 44458 Da [This is the MW of the unprocessed precursor]

CRC64: 926B9FC8625E20CD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALVVQKYGG SSVADAERIR RVAERIVETK KAGNDVVVVV SAMGDTTDDL LDLARQVSPA 

        70         80         90        100        110        120 
PPPREMDMLL TAGERISNAL VAMAIESLGA QARSFTGSQA GVITTGTHGN AKIIDVTPGR 

       130        140        150        160        170        180 
LRDALDEGQI VLVAGFQGVS QDSKDVTTLG RGGSDTTAVA VAAALDADVC EIYTDVDGIF 

       190        200        210        220        230        240 
TADPRIVPNA RHLDTVSFEE MLEMAACGAK VLMLRCVEYA RRYNVPIHVR SSYSDKPGTI 

       250        260        270        280        290        300 
VKGSIEDIPM EDAILTGVAH DRSEAKVTVV GLPDVPGYAA KVFRAVAEAD VNIDMVLQNI 

       310        320        330        340        350        360 
SKIEDGKTDI TFTCARDNGP RAVEKLSALK SEIGFSQVLY DDHIGKVSLI GAGMRSHPGV 

       370        380        390        400        410        420 
TATFCEALAE AGINIDLIST SEIRISVLIK DTELDKAVSA LHEAFGLGGD DEAVVYAGTG 


R

P41403 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