NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=1444390 [NCBI, ExPASy, EBI, Israel, Japan]
Schendel F.J., Flickinger M.C.;
"Cloning and nucleotide sequence of the gene coding for aspartokinase II from a thermophilic methylotrophic Bacillus sp.";
Appl. Environ. Microbiol. 58:2806-2814(1992).

Comments

CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-aspartate.
ENZYME REGULATION: Lysine-sensitive.
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	Q59229-1
This is the isoform sequence displayed in this entry.

Name	Beta
Synonyms	Aspartokinase 2 subunit beta
Isoform ID	Q59229-2
Features which should be applied to build the isoform sequence: VSP_018653.

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

M93419; AAA22251.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q59229.

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: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.

ProtoNet

Q59229.

Other

UniRef

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

Keywords

Alternative initiation; Amino-acid biosynthesis; Diaminopimelate biosynthesis; Direct protein sequencing; Kinase; Lysine biosynthesis; Repeat; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 411`	`411`	`Aspartokinase 2.`	`PRO_0000002369`
`DOMAIN`	`263 336`	`74`	`ACT 1.`
`DOMAIN`	`343 408`	`66`	`ACT 2.`
`VAR_SEQ`	`1 245`		`Missing (in isoform Beta).`	`VSP_018653`

Sequence information

Length: 411 AA [This is the length of the unprocessed precursor]

Molecular weight: 44343 Da [This is the MW of the unprocessed precursor]

CRC64: 94061572E369CD48 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGLIVQKFGG TSVGSVERIL NVANRVIEEK KNGNDVVVVV SAMGKTTDEL VDLAKQISAH 

        70         80         90        100        110        120 
PPKREMDMLL TTGEQVTISL LAMALNEKGY EAISYTGWQA GITTEPVFGN ARILNIETEK 

       130        140        150        160        170        180 
IQKQLNEGKI VVVAGFQGID EHGEITTLGR GGSDTTAVAL AAALKAEKCD IYTDVTGVFT 

       190        200        210        220        230        240 
TDPRYVKSAR KLASISYDEM LELANLGAGV LHPRAVEFAK NYGITLEVRS SMEREEGTII 

       250        260        270        280        290        300 
EEEVTMEQNL VVRGVAFEDE ITRVTVFGLP NSLTSLSTIF TTLAQNRINV DIIIQSATDA 

       310        320        330        340        350        360 
ETTNLSFSIK SDDLEETMAV LENNKNLLNY QGIESETGLA KVSIVGSGMI SNPGVAAKMF 

       370        380        390        400        410 
EVLALNGIQV KMVSTSEIKV STVVEESQMI KAVEALHQAF ELSGSAVKSE R

Q59229 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