NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 33923 / DSM 674 / AT-62;
PubMed=7773416 [NCBI, ExPASy, EBI, Israel, Japan]
Nishiyama M., Kukimoto M., Beppu T., Horiouchi S.;
"An operon encoding aspartokinase and purine phosphoribosyltransferase in Thermus flavus.";
Microbiology 141:1211-1219(1995).

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	P61489-1
This is the isoform sequence displayed in this entry.

Name	Beta
Synonyms	Aspartokinase subunit beta
Isoform ID	P61489-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_018665.

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

D37928; BAA07146.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D37928; BAA07147.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

2DT9; X-ray; 2.15 A; A/B=245-405.

[ExPASy / RCSB / EBI]

PDBsum

2DT9; -.

ModBase

P61489.

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

3D-structure; 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`	`1 405`	`405`	`Aspartokinase.`	`PRO_0000002389`
`DOMAIN`	`262 335`	`74`	`ACT 1.`
`DOMAIN`	`343 404`	`62`	`ACT 2.`
`VAR_SEQ`	`1 244`		`Missing (in isoform Beta).`	`VSP_018665`

Sequence information

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

Molecular weight: 43319 Da [This is the MW of the unprocessed precursor]

CRC64: 47A3A29E2B82D0EA [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 
IREALDQGFV 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

P61489 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