[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=NUB3621; DOI=10.1016/0378-1119(95)00834-9; PubMed=8635739 [NCBI, ExPASy, EBI, Israel, Japan] Cantoni R., Labo M., de Rossi E., Riccardi G.; "Sequence of the Bacillus stearothermophilus gene encoding aspartokinase II."; Gene 169:135-136(1996).

Comments

CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-aspartate.
ENZYME REGULATION: Lysine-sensitive (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).

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

Name	Alpha
Synonyms	Aspartokinase 2 subunit alpha
Isoform ID	P53553-1
This is the isoform sequence displayed in this entry.

Name	Beta
Synonyms	Aspartokinase 2 subunit beta
Isoform ID	P53553-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_018654.

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

L46351; AAB06216.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC4640; JC4640.

3D structure databases

ModBase

P53553.

Ontologies

GO:0019877;	Biological process: diaminopimelate biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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`	`1 407`	`407`	`Aspartokinase 2.`	`PRO_0000002371`
`DOMAIN`	`262 335`	`74`	`ACT 1.`
`DOMAIN`	`339 404`	`66`	`ACT 2.`
`VAR_SEQ`	`1 245`		`Missing (in isoform Beta).`	`VSP_018654`

Sequence information

Length: 407 AA [This is the length of the unprocessed precursor]

Molecular weight: 44002 Da [This is the MW of the unprocessed precursor]

CRC64: 2A848E6A7037B172 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGIIVQKFGG TSVGSIERIQ HVANRVIEEV QKGNDVVVVV SAMGKTTDEL VNLAKQISNH 

        70         80         90        100        110        120 
PSKREMDMLL STGEQVSIAL LAMSLHEKGY KAVSLTGWQA GITTEEMHGN ARIMNIDTTR 

       130        140        150        160        170        180 
IRRCLDEGAI VIVAGFQGVT ETGEITTLGR GGSDTTAVAL AAALKAEKCD IYTDVTGVFT 

       190        200        210        220        230        240 
TDPRYVKTAR KIKEISYDEM LELANLGAGV LHPRAVEFAK NYEVPLEVRS SMENERGTMV 

       250        260        270        280        290        300 
KEEVSMEQHL IVRGIAFEDQ VTRVTVVGIE KYLQSVATIF TALANRGINV DIIIQNATNS 

       310        320        330        340        350        360 
ETASVSFSIR TEDLPETLQV LQALEGADVH YESGLAKVSI VGSGMISNPG VAARVFEVLA 

       370        380        390        400 
DQGIEIKMVS ISEIKISTVI DEKYMVSAVE ELHEAFGLAE EAAAVRS

P53553 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