NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BCG / Pasteur;
DOI=10.1111/j.1365-2958.1994.tb00342.x; PubMed=7910936 [NCBI, ExPASy, EBI, Israel, Japan]
Cirillo J.D., Weisbrod T.R., Pascopella L., Bloom B.R., Jacobs W.R. Jr.;
"Isolation and characterization of the aspartokinase and aspartate semialdehyde dehydrogenase operon from mycobacteria.";
Mol. Microbiol. 11:629-639(1994).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-935 / AF2122/97;
DOI=10.1073/pnas.1130426100; PubMed=12788972 [NCBI, ExPASy, EBI, Israel, Japan]
Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
"The complete genome sequence of Mycobacterium bovis.";
Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).

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.
SEQUENCE CAUTION:
- Sequence=Z18290; Type=Frameshift; Positions=313;

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

Z18290; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
BX248347; CAD95921.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_857373.1; -.

3D structure databases

HSSP

P00353; 1BRM. [HSSP ENTRY / PDB]

ModBase

P0A543.

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; 1.

Genome annotation databases

GeneID

1093103; -.

GenomeReviews

BX248333_GR; Mb3735c.

KEGG

mbo:Mb3735c; -.

Phylogenomic databases

HOGENOM

P0A543; -.

Genome annotation databases

CMR

P0A543; Mb3735c.

Other

ProtoNet

P0A543.

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`	`1 345`	`345`	`Aspartate-semialdehyde dehydrogenase.`	`PRO_0000141381`
`ACT_SITE`	`130 130`		`Acyl-thioester intermediate (By similarity).`

Sequence information

Length: 345 AA [This is the length of the unprocessed precursor]

Molecular weight: 36230 Da [This is the MW of the unprocessed precursor]

CRC64: C886DDB63D03E25D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGLSIGIVGA TGQVGQVMRT LLDERDFPAS AVRFFASARS QGRKLAFRGQ EIEVEDAETA 

        70         80         90        100        110        120 
DPSGLDIALF SAGSAMSKVQ APRFAAAGVT VIDNSSAWRK DPDVPLVVSE VNFERDAHRR 

       130        140        150        160        170        180 
PKGIIANPNC TTMAAMPVLK VLHDEARLVR LVVSSYQAVS GSGLAGVAEL AEQARAVIGG 

       190        200        210        220        230        240 
AEQLVYDGGA LEFPPPNTYV APIAFNVVPL AGSLVDDGSG ETDEDQKLRF ESRKILGIPD 

       250        260        270        280        290        300 
LLVSGTCVRV PVFTGHSLSI NAEFAQPLSP ERARELLDGA TGVQLVDVPT PLAAAGVDES 

       310        320        330        340 
LVGRIRRDPG VPDGRGLALF VSGDNLRKGA ALNTIQIAEL LTADL

P0A543 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