NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2434499 [NCBI, ExPASy, EBI, Israel, Japan]
Cardineau G.A., Curtiss R. III;
"Nucleotide sequence of the asd gene of Streptococcus mutans. Identification of the promoter region and evidence for attenuator-like sequences preceding the structural gene.";
J. Biol. Chem. 262:3344-3353(1987).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700610 / UA159 / Serotype c;
DOI=10.1073/pnas.172501299; PubMed=12397186 [NCBI, ExPASy, EBI, Israel, Japan]
Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen.";
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).

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

J02667; AAA26850.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014133; AAN58690.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A29137; A29137.

RefSeq

NP_721384.1; -.

3D structure databases

HSSP

P00353; 1BRM. [HSSP ENTRY / PDB]

SMR

P10539; 2-358.

ModBase

P10539.

Enzyme and pathway databases

BioCyc

SMUT210007:SMU_989-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; 1.

Genome annotation databases

GeneID

1028321; -.

GenomeReviews

AE014133_GR; SMU_989.

KEGG

smu:SMU.989; -.

NMPDR

fig|210007.1.peg.897; -.

Phylogenomic databases

HOGENOM

P10539; -.

Genome annotation databases

CMR

P10539; SMU_989.

Other

ProtoNet

P10539.

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`	`1 358`	`358`	`Aspartate-semialdehyde dehydrogenase.`	`PRO_0000141392`
`ACT_SITE`	`128 128`		`Acyl-thioester intermediate (By similarity).`
`CONFLICT`	`64 64`		`G -> A (in Ref. 1; AAA26850).`
`CONFLICT`	`190 190`		`L -> F (in Ref. 1; AAA26850).`
`CONFLICT`	`242 242`		`T -> H (in Ref. 1; AAA26850).`
`CONFLICT`	`301 301`		`Missing (in Ref. 1; AAA26850).`
`CONFLICT`	`335 340`		`VQIAES -> IITANR (in Ref. 1; AAA26850).`

Sequence information

Length: 358 AA [This is the length of the unprocessed precursor]

Molecular weight: 38903 Da [This is the MW of the unprocessed precursor]

CRC64: 11F5E4AD52C1A40B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGYTVAIVGA TGAVGTRMIQ QLEQSTLPVD KVRLLSSSRS AGKVLQYKDQ DVTVELTTKD 

        70         80         90        100        110        120 
SFEGVDIALF SAGGSVSAKF APYAVKAGAV VVDNTSHFRQ NPDVPLVVPE VNAYAMDAHN 

       130        140        150        160        170        180 
GIIACPNCST IQMMVALEPI RQKWGLSRVI VSTYQAVSGA GQSAINETVR EIKEVVNDGV 

       190        200        210        220        230        240 
DPKAVHADIL PSGGDKKHYP IAFNALAQID VFTDNDYTYE EMKMTNETKK IMEEPELPVS 

       250        260        270        280        290        300 
ATCVRVPILF SHSEAVYIET KDVAPIEEVK AAIAAFPGAV LEDDIKHQIY PQAANAVGSR 

       310        320        330        340        350 
ETFVGRIRKD LDIENGIHMW VVSDNLLKGA AWNSVQIAES LHERGLVRST SELKFELK

P10539 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