NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=AA100 / Serogroup 1;
PubMed=9573067 [NCBI, ExPASy, EBI, Israel, Japan]
Harb O.S., Abu Kwaik Y.;
"Identification of the aspartate-beta-semialdehyde dehydrogenase gene of Legionella pneumophila and characterization of a null mutant.";
Infect. Immun. 66:1898-1903(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

AF034213; AAC46292.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P00353; 1BRM. [HSSP ENTRY / PDB]

ModBase

O31219.

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.

Other

ProtoNet

O31219.

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 347`	`347`	`Aspartate-semialdehyde dehydrogenase.`	`PRO_0000141378`
`ACT_SITE`	`132 132`		`Acyl-thioester intermediate (By similarity).`

Sequence information

Length: 347 AA [This is the length of the unprocessed precursor]

Molecular weight: 37714 Da [This is the MW of the unprocessed precursor]

CRC64: 33D992101D707943 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSRHLNVAIV GATGAVGETF LTVLEERNFP IKSLYPLASS RSVGKTVTFR DQELDVLDLA 

        70         80         90        100        110        120 
EFDFSKVDLA LFSAGGAVSK EYAPKAVAAG CVVVDNTSCF RYEDDIPLVV PGSESSSNRD 

       130        140        150        160        170        180 
YTKRGIIANP NCSTIQMVVA LKPIYDAVGI SRINVATYQS VSGTGKKAIS ELVAQVGDLL 

       190        200        210        220        230        240 
NGRPANVQVY PQQIAFNALP HIDQFEDNGY TREEMKMVWE TRKIMEDDSI MVNPTAVRVP 

       250        260        270        280        290        300 
VIYGHSEAVH LELKKPLTAD DARALLAKAP GVTVVDNLSK ASYPTAIKNA VGHDDVFVGR 

       310        320        330        340 
IRQDISHPCG LNLWIVADNI RKGAATNAVQ IAEILQREFL LKLSLPQ

O31219 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