Aspartate-semialdehyde dehydrogenase - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0A9Q9 (DHAS_ECOLI)

Last modified June 16, 2009. Version 43. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Aspartate-semialdehyde dehydrogenase
      Short name=ASA dehydrogenase
      Short name=ASADH
    EC=1.2.1.11

Gene names

Name:	asd
Synonyms:	hom
Ordered Locus Names:	b3433, JW3396

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	367 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (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. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the aspartate-semialdehyde dehydrogenase family.

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Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	diaminopimelate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro NADP or NADPH binding Inferred from electronic annotation. Source: InterPro aspartate-semialdehyde dehydrogenase activity Inferred from electronic annotation. Source: EC protein dimerization activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
dnaK	P0A6Y8	1	EBI-1132825,EBI-542092

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 367

367

Aspartate-semialdehyde dehydrogenase

PRO_0000141369

Sites

Active site

135

Acyl-thioester intermediate

Binding site

135

Cysteine (covalent); in inhibited form

Experimental info

Mutagenesis

135

C → A: Complete loss of activity. Ref.5

Mutagenesis

135

C → S: 99.7% loss of activity. Ref.5

Sequence conflict

W → G AA sequence Ref.4

Secondary structure

367

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P0A9Q9-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: F53D4C36EA7CC201
Show »

FASTA

367

40,018

        10         20         30         40         50         60 
MKNVGFIGWR GMVGSVLMQR MVEERDFDAI RPVFFSTSQL GQAAPSFGGT TGTLQDAFDL 

        70         80         90        100        110        120 
EALKALDIIV TCQGGDYTNE IYPKLRESGW QGYWIDAASS LRMKDDAIII LDPVNQDVIT 

       130        140        150        160        170        180 
DGLNNGIRTF VGGNCTVSLM LMSLGGLFAN DLVDWVSVAT YQAASGGGAR HMRELLTQMG 

       190        200        210        220        230        240 
HLYGHVADEL ATPSSAILDI ERKVTTLTRS GELPVDNFGV PLAGSLIPWI DKQLDNGQSR 

       250        260        270        280        290        300 
EEWKGQAETN KILNTSSVIP VDGLCVRVGA LRCHSQAFTI KLKKDVSIPT VEELLAAHNP 

       310        320        330        340        350        360 
WAKVVPNDRE ITMRELTPAA VTGTLTTPVG RLRKLNMGPE FLSAFTVGDQ LLWGAAEPLR 


RMLRQLA

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the asd gene of Escherichia coli: absence of a typical attenuation signal." Haziza C., Stragier P., Patte J.-C. EMBO J. 1:379-384(1982) [PubMed: 6143662] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-12. Strain: K12 / EMG2.
[5]	"Identification of an essential cysteine in the reaction catalyzed by aspartate-beta-semialdehyde dehydrogenase from Escherichia coli." Karsten W.E., Viola R.E. Biochim. Biophys. Acta 1121:234-238(1992) [PubMed: 1350921] [Abstract] Cited for: MUTAGENESIS OF CYS-135.
[6]	"L-cystine inhibits aspartate-beta-semialdehyde dehydrogenase by covalently binding to the essential 135Cys of the enzyme." Alvarez E., Ramon F., Magan C., Diez E. Biochim. Biophys. Acta 1696:23-29(2004) [PubMed: 14726201] [Abstract] Cited for: INHIBITION BY CYSTEINE BINDING AT CYS-135.
[7]	"Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis." Hadfield A., Kryger G., Ouyang J., Petsko G.A., Ringe D., Viola R. J. Mol. Biol. 289:991-1002(1999) [PubMed: 10369777] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

V00262 Genomic DNA. Translation: CAA23511.1.
U18997 Genomic DNA. Translation: AAA58231.1.
U00096 Genomic DNA. Translation: AAC76458.1.
AP009048 Genomic DNA. Translation: BAE77859.1.

PIR

DEECDA. A00364.

RefSeq

AP_004358.1.
NP_417891.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BRM	X-ray	2.50	A/B/C	1-367	[»]
1GL3	X-ray	2.60	A/B	1-367	[»]
1T4B	X-ray	1.60	A/B	3-367	[»]
1T4D	X-ray	1.95	A/B/C	3-367	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A9Q9. 1 interaction.

PTM databases

PhosSite

P0A9Q9.

2-D gel databases

SWISS-2DPAGE

P0A9Q9.

2DBase-Ecoli

P0A9Q9.

Genome annotation databases

GeneID

947939.

GenomeReviews

Gene locus JW3396 in contig AP009048_GR.
Gene locus b3433 in contig U00096_GR.

KEGG

ecj:JW3396.
eco:b3433.

Organism-specific databases

EchoBASE

EB0086.

EcoGene

EG10088. asd.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A9Q9.

OMA

P0A9Q9. IDGLCVR.

Enzyme and pathway databases

BioCyc

EcoCyc:ASP-SEMIALDEHYDE-DEHYDROGENASE-MON.
MetaCyc:ASP-SEMIALDEHYDE-DEHYDROGENASE-MON.

Family and domain databases

InterPro

IPR000319. Asp-semialdehyde_DH_CS.
IPR011534. Asp_ADH_proteob.
IPR012080. Asp_semialdehyde_DH.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
IPR012280. Semialdhyde_DH_C.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

Pfam

PF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view]

PIRSF

PIRSF000148. ASA_dh. 1 hit.

TIGRFAMs

TIGR01745. asd_gamma. 1 hit.

PROSITE

PS01103. ASD. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

DHAS_ECOLI

Accession

Primary (citable) accession number: P0A9Q9
Secondary accession number(s): P00353, Q2M797

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents