NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/dnares/2.4.153; PubMed=8590279 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S.;
"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome.";
DNA Res. 2:153-166(1995).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/dnares/3.3.109; PubMed=8905231 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions.";
DNA Res. 3:109-136(1996).

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

BA000022; BAA10869.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S76022; S76022.

RefSeq

NP_442798.1; -.

3D structure databases

ModBase

Q55512.

Protein-protein interaction databases

IntAct

Q55512; -.

Enzyme and pathway databases

BioCyc

SSP1148:SLR0549-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 EC).
GO:0051287;	Molecular function: NAD 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:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000319; Asp-semialdehyde_DHase_CS.
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.

PROSITE

PS01103; ASD; FALSE_NEG.

ProtoNet

Q55512.

Genome annotation databases

GeneID

952082; -.

GenomeReviews

BA000022_GR; slr0549.

KEGG

syn:slr0549; -.

NMPDR

fig|1148.1.peg.2899; -.

Phylogenomic databases

HOGENOM

Q55512; -.

Genome annotation databases

CMR

Q55512; slr0549.

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`	`1 280`	`280`	`Aspartate-semialdehyde dehydrogenase.`	`PRO_0000141393`
`ACT_SITE`	`72 72`		`Acyl-thioester intermediate (By similarity).`

Sequence information

Length: 280 AA [This is the length of the unprocessed precursor]

Molecular weight: 30605 Da [This is the MW of the unprocessed precursor]

CRC64: 3335A9BB4A6FFB7B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDGSAFKGCD LVLASAGGST SKRWAEEITK AGAVMVDNSS AFRMVPEVPL VVPEINPEAA 

        70         80         90        100        110        120 
QNHQGIIANP NCTTILMGVA IYPLHQLQPI KRIVVATYQS ASGAGAMAME EVKHQSRDIL 

       130        140        150        160        170        180 
EGKIPQAEIL PYPLAFNLFP HNSPITANHY CEEEMKMVQE TRKIFAAEDI RITATCVRVP 

       190        200        210        220        230        240 
VLRAHSEAVN LEFATPFPVE LAKTAIAKAP GVKLVEDWQK NYFPMPMDAT GQDDVLVGRI 

       250        260        270        280 
RQDISHPNGL DLWLCGDQIR KGAALNAVQI AELLVERGWL

Q55512 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