NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Madrid E;
DOI=10.1038/24094; PubMed=9823893 [NCBI, ExPASy, EBI, Israel, Japan]
Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G.;
"The genome sequence of Rickettsia prowazekii and the origin of mitochondria.";
Nature 396:133-140(1998).

Comments

CATALYTIC ACTIVITY: L-aspartate 4-semialdehyde + phosphate + NADP⁺ = L-4-aspartyl phosphate + NADPH.
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; tetrahydrodipicolinate from L-aspartate: step 2/4 .
PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3 .
PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5 .
SUBUNIT: Homodimer (By similarity).
SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase 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

AJ235271; CAA14776.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

F71687; F71687.

RefSeq

NP_220699.1; -.

3D structure databases

ModBase

Q9ZDL2.

Enzyme and pathway databases

BioCyc

RPRO272947:RP316-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0004073;	Molecular function: aspartate-semialdehyde dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0046983;	Molecular function: protein dimerization activity (inferred from electronic annotation from InterPro).
GO:0019877;	Biological process: diaminopimelate biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0009086;	Biological process: methionine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009088;	Biological process: threonine biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000319; Asp-semialdehyde_DHase_CS.
IPR012080; Asp_semialdehyde_DHase.
IPR005986; Asp_semialdehyde_DHase_bac.
IPR000534; Semialdehyde_DHase_NAD-bd.
IPR012280; Semialdhyde_DHase_C.
Graphical view of domain structure.

Pfam

PF01118; Semialdhyde_dh; 1.
PF02774; Semialdhyde_dhC; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000148; ASA_dh; 1.

TIGRFAMs

TIGR01296; asd_B; 1.

PROSITE

PS01103; ASD; FALSE_NEG.

ProtoNet

Q9ZDL2.

Genome annotation databases

GeneID

883494; -.

GenomeReviews

AJ235269_GR; RP316.

KEGG

rpr:RP316; -.

Phylogenomic databases

HOGENOM

Q9ZDL2; -.

Genome annotation databases

CMR

Q9ZDL2; RP316.

Other

UniRef

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

Keywords

Amino-acid biosynthesis; Complete proteome; Diaminopimelate biosynthesis; Lysine biosynthesis; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 338`	`338`	`Aspartate-semialdehyde dehydrogenase.`	`PRO_0000141388`
`ACT_SITE`	`132 132`		`Acyl-thioester intermediate (By similarity).`

Sequence information

Length: 338 AA [This is the length of the unprocessed precursor]

Molecular weight: 37668 Da [This is the MW of the unprocessed precursor]

CRC64: 61E4CE8DDAD7A20E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTKKYNIAVI GATGNVGRET LNILAERHFP INKIYAIASD NSLGREVRFG EKILHINSIK 

        70         80         90        100        110        120 
IFNFHDIEIA FFCAGSNVSK EFIPKATSCN CIVIDKTSLF RADNQVPLIV PEVNLSTLKE 

       130        140        150        160        170        180 
FNTKNIIANP NCIVIPLVVV LKPLDNEIKI KRVVISTYQS VSGAGKAGMD ELYNQTKSKY 

       190        200        210        220        230        240 
VFRENNPKKF PKQIAFNLFP YIGDLNKDGY TSEETKIAFE LNKIMGNHFK TSVTSVRVPV 

       250        260        270        280        290        300 
FIGHAISVNI EFSDKIYAKD VEEILQDADG IVTISNNNGL AYISPIEVVG EDAVYVSRIR 

       310        320        330 
NDLSKDNTIN LWITCDNLRK GAALNSVQIA EALINNYL

Q9ZDL2 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