NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10074061 [NCBI, ExPASy, EBI, Israel, Japan]
Kobashi N., Nishiyama M., Tanokura M.;
"Aspartate kinase-independent lysine synthesis in an extremely thermophilic bacterium, Thermus thermophilus: lysine is synthesized via alpha-aminoadipic acid not via diaminopimelic acid.";
J. Bacteriol. 181:1713-1718(1999).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nbt956; PubMed=15064768 [NCBI, ExPASy, EBI, Israel, Japan]
Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
"The genome sequence of the extreme thermophile Thermus thermophilus.";
Nat. Biotechnol. 22:547-553(2004).

Comments

CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-aspartate.
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	P61488-1
This is the isoform sequence displayed in this entry.

Name	Beta
Synonyms	Aspartokinase subunit beta
Isoform ID	P61488-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_018664.

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

AB013131; BAA25848.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB013131; BAA25849.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE017221; AAS80514.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_004141.1; -.

3D structure databases

ModBase

P61488.

Enzyme and pathway databases

BioCyc

TTHE262724:TT_C0166-MON; -.

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

P61488.

Genome annotation databases

GeneID

2775578; -.

GenomeReviews

AE017221_GR; TT_C0166.

Phylogenomic databases

HOGENOM

P61488; -.

Genome annotation databases

CMR

P61488; TT_C0166.

Other

UniRef

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

Keywords

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`	`1 405`	`405`	`Aspartokinase.`	`PRO_0000002387`
`DOMAIN`	`262 335`	`74`	`ACT 1.`
`DOMAIN`	`343 404`	`62`	`ACT 2.`
`VAR_SEQ`	`1 244`		`Missing (in isoform Beta).`	`VSP_018664`

Sequence information

Length: 405 AA [This is the length of the unprocessed precursor]

Molecular weight: 43333 Da [This is the MW of the unprocessed precursor]

CRC64: 06F7B79E908960EA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALVVQKYGG TSVGDLERIH KVAQRIAHYR EKGHRLAVVV SAMGHTTDEL IALAKRVNPR 

        70         80         90        100        110        120 
PPFRELDLLT TTGEQVSVAL LSMQLWAMGI PAKGFVQHQI GITTDGRYGD ARILEVNPAR 

       130        140        150        160        170        180 
IREALEQGFV AVIAGFMGTT PEGEITTLGR GGSDTTAVAI AAALGAKECE IYTDTEGVYT 

       190        200        210        220        230        240 
TDPHLIPEAR KLSVIGYDQM LEMAALGARV LHPRAVYYAK RYGVVLHVRS SFSYNPGTLV 

       250        260        270        280        290        300 
KEVAMEMDKA VTGVALDLDH AQIGLIGIPD QPGIAAKVFQ ALAERGIAVD MIIQGVPGHD 

       310        320        330        340        350        360 
PSRQQMAFTV KKDFAQEALE ALEPVLAEIG GEAILRPDIA KVSIVGVGLA STPEVPAKMF 

       370        380        390        400 
QAVASTGANI EMIATSEVRI SVIIPAEYAE AALRAVHQAF ELDKA

P61488 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