NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pgen.0020076; PubMed=16703114 [NCBI, ExPASy, EBI, Israel, Japan]
Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D.;
"Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens.";
PLoS Genet. 2:733-744(2006).

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 .
SIMILARITY: Belongs to the aspartokinase family.

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

CP000087; ABE05485.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_538574.1; -.

3D structure databases

ModBase

Q1RGM9.

Enzyme and pathway databases

BioCyc

RBEL336407:RBE_1404-MON; -.

Ontologies

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

IPR001048; Asp/Glu/Uridylate_kinase.
IPR001341; Asp_kin_reg.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.1160.10; Aa_kinase; 1.

Pfam

PF00696; AA_kinase; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00657; asp_kinases; 1.

PROSITE

PS00324; ASPARTOKINASE; 1.

ProtoNet

Q1RGM9.

Genome annotation databases

GeneID

3995472; -.

GenomeReviews

CP000087_GR; RBE_1404.

KEGG

rbe:RBE_1404; -.

Phylogenomic databases

HOGENOM

Q1RGM9; -.

Genome annotation databases

CMR

Q1RGM9; RBE_1404.

Other

UniRef

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

Keywords

Amino-acid biosynthesis; Complete proteome; Diaminopimelate biosynthesis; Kinase; Lysine biosynthesis; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 406`	`406`		`Aspartokinase.`	`PRO_0000288718`

Sequence information

Length: 406 AA [This is the length of the unprocessed precursor]

Molecular weight: 44682 Da [This is the MW of the unprocessed precursor]

CRC64: 8A27CD8A2A864AC6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALIIQKFGG TSVTTIDRIK KIIPIIKAEI AKNNQVIIVV SAMAGVTNQL VTLCNEVSSL 

        70         80         90        100        110        120 
NKSSQLAEYD VALSSGEIVT ASLLALALQE ENINARSFLA WQLPILTDDN HSKALVESVD 

       130        140        150        160        170        180 
TNLLNECLQQ NIIPIIAGFQ GINKHNRLAT LGRGGSDTTA ALIAAAMKAD RCDIYTDVEG 

       190        200        210        220        230        240 
VFAADPRIIP KAKKIDEIDF SEMLELALSG AKVLHSRAAE IVMRYQIDMR ILSTFAPEAG 

       250        260        270        280        290        300 
CTLITSKDKI MEKRIISGIT SNKNLLYITI ESSSLNFIQV ASIIAQNNNH IEVMQEIEPN 

       310        320        330        340        350        360 
KRYSFITNLT DKNSLHILLT NLKNNNQISN FTFDTEIATV SIIGHGIKND LKLLEVILSK 

       370        380        390        400 
LAKDNINVQM VQISEIKIIL LINDKQVEKT VLDLYDLLKI SETGHC

Q1RGM9 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