ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P0A9Q9


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name DHAS_ECOLI
Primary accession number P0A9Q9
Secondary accession numbers P00353 Q2M797
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 38)
Name and origin of the protein
Protein name Aspartate-semialdehyde dehydrogenase
Synonyms ASA dehydrogenase
ASADH
EC 1.2.1.11
Gene name
Name: asd
Synonyms: hom
OrderedLocusNames: b3433, JW3396
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6143662 [NCBI, ExPASy, EBI, Israel, Japan]
Haziza C., Stragier P., Patte J.-C.;
"Nucleotide sequence of the asd gene of Escherichia coli: absence of a typical attenuation signal.";
EMBO J. 1:379-384(1982).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
PROTEIN SEQUENCE OF 1-12.
STRAIN=K12 / EMG2;
DOI=10.1002/elps.1150180807; PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[5]
MUTAGENESIS OF CYS-135.
DOI=10.1016/0167-4838(92)90360-P; PubMed=1350921 [NCBI, ExPASy, EBI, Israel, Japan]
Karsten W.E., Viola R.E.;
"Identification of an essential cysteine in the reaction catalyzed by aspartate-beta-semialdehyde dehydrogenase from Escherichia coli.";
Biochim. Biophys. Acta 1121:234-238(1992).
[6]
INHIBITION BY CYSTEINE BINDING AT CYS-135.
DOI=10.1016/j.bbapap.2003.09.002; PubMed=14726201 [NCBI, ExPASy, EBI, Israel, Japan]
Alvarez E., Ramon F., Magan C., Diez E.;
"L-cystine inhibits aspartate-beta-semialdehyde dehydrogenase by covalently binding to the essential 135Cys of the enzyme.";
Biochim. Biophys. Acta 1696:23-29(2004).
[7]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1006/jmbi.1999.2828; PubMed=10369777 [NCBI, ExPASy, EBI, Israel, Japan]
Hadfield A., Kryger G., Ouyang J., Petsko G.A., Ringe D., Viola R.;
"Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis.";
J. Mol. Biol. 289:991-1002(1999).
Comments
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
V00262; CAA23511.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U18997; AAA58231.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76458.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77859.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A00364; DEECDA.
RefSeq AP_004358.1; -.
NP_417891.1; -.
3D structure databases
PDB
1BRM; X-ray; 2.50 A; A/B/C=1-367.[ExPASy / RCSB / EBI]
1GL3; X-ray; 2.60 A; A/B=1-367.[ExPASy / RCSB / EBI]
1T4B; X-ray; 1.60 A; A/B=1-367.[ExPASy / RCSB / EBI]
1T4D; X-ray; 1.95 A; A/B/C=1-367.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BRM; -.
1GL3; -.
1T4B; -.
1T4D; -.
ModBase P0A9Q9.
Protein-protein interaction databases
IntAct P0A9Q9; 1.
Enzyme and pathway databases
BioCyc EcoCyc:ASP-SEMIALDEHYDE-DEHYDROGENASE-MON; -.
MetaCyc:ASP-SEMIALDEHYDE-DEHYDROGENASE-MON; -.
2D gel databases
SWISS-2DPAGE P0A9Q9; -.
2DBase-Ecoli P0A9Q9; -.
Organism-specific databases
EchoBASE EB0086; -.
EcoGene EG10088; asd.
Ontologies
GO
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:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000319; Asp-semialdehyde_DHase_CS.
IPR011534; Asp_ADH_proteob.
IPR012080; Asp_semialdehyde_DHase.
IPR016040; NAD(P)-bd.
IPR000534; Semialdehyde_DHase_NAD-bd.
IPR012280; Semialdhyde_DHase_C.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF01118; Semialdhyde_dh; 1.
PF02774; Semialdhyde_dhC; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000148; ASA_dh; 1.
TIGRFAMs TIGR01745; asd_gamma; 1.
PROSITE PS01103; ASD; 1.
Genome annotation databases
GeneID 947939; -.
GenomeReviews AP009048_GR; JW3396.
U00096_GR; b3433.
KEGG ecj:JW3396; -.
eco:b3433; -.
Phylogenomic databases
HOGENOM P0A9Q9; -.
Other
LinkHub P0A9Q9; -.
Genome annotation databases
CMR P0A9Q9; b3433.
Other
ProtoNet P0A9Q9.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Amino-acid biosynthesis; Complete proteome; Diaminopimelate biosynthesis; Direct protein sequencing; Lysine biosynthesis; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   367  367     Aspartate-semialdehyde dehydrogenase. PRO_0000141369
ACT_SITE   135   135        Acyl-thioester intermediate. 
BINDING   135   135        Cysteine (covalent); in inhibited form. 
MUTAGEN   135   135        C->A: Complete loss of activity. 
MUTAGEN   135   135        C->S: 99.7% loss of activity. 
CONFLICT   9     9        W -> G (in Ref. 4; AA sequence). 
STRAND   3     8  6      
HELIX   12    23  12      
HELIX   26    29  4      
STRAND   30    39  10      
HELIX   46    48  3      
HELIX   60    64  5      
STRAND   67    71  5      
HELIX   75    87  13      
STRAND   93    96  4      
TURN   100   103  4      
STRAND   107   110  4      
HELIX   112   124  13      
STRAND   129   132  4      
HELIX   135   149  15      
STRAND   153   162  10      
HELIX   164   166  3      
HELIX   169   185  17      
HELIX   187   190  4      
HELIX   197   210  14      
TURN   216   218  3      
STRAND   226   228  3      
HELIX   240   253  14      
STRAND   261   264  4      
STRAND   267   269  3      
STRAND   271   284  14      
HELIX   288   298  11      
HELIX   309   315  7      
HELIX   318   321  4      
STRAND   329   334  6      
STRAND   341   349  9      
HELIX   352   356  5      
HELIX   357   366  10      
Sequence information
Length: 367 AA [This is the length of the unprocessed precursor] Molecular weight: 40018 Da [This is the MW of the unprocessed precursor] CRC64: F53D4C36EA7CC201 [This is a checksum on the sequence]
        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 

P0A9Q9 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 logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!