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 Q56734


[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_SHEVI
Primary accession number Q56734
Secondary accession numbers None
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 53)
Name and origin of the protein
Protein name Aspartate-semialdehyde dehydrogenase
Synonyms ASA dehydrogenase
ASADH
EC 1.2.1.11
Gene name
Name: asd
From
Shewanella violacea [TaxID: 60217] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; Shewanellaceae; Shewanella.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DSS12;
PubMed=9163523 [NCBI, ExPASy, EBI, Israel, Japan]
Kato C., Smorawinska M., Li L., Horikoshi K.;
"Comparison of the gene expression of aspartate beta-D-semialdehyde dehydrogenase at elevated hydrostatic pressure in deep-sea bacteria.";
J. Biochem. 121:717-723(1997).
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
D49540; BAA08490.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JC5436; JC5436.
3D structure databases
HSSP P00353; 1BRM. [HSSP ENTRY / PDB]
ModBase Q56734.
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: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.
ProtoNet Q56734.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Diaminopimelate biosynthesis; Lysine biosynthesis; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   338  338     Aspartate-semialdehyde dehydrogenase. PRO_0000141390
ACT_SITE   132   132        Acyl-thioester intermediate (By similarity). 
Sequence information
Length: 338 AA [This is the length of the unprocessed precursor] Molecular weight: 37061 Da [This is the MW of the unprocessed precursor] CRC64: 8D0DC1F46EAF30AC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSQEFNVVVL GASGAVGQTM IEILEERNFP VAKLFPLASS RSAGGTVSFN GKQVEILDVD 

        70         80         90        100        110        120 
DFDWSQAQIG FFSAGGDVSE KWAPIAAENG CVVIDNTSQF RYDNDVPLVI PEVNPEAIAD 

       130        140        150        160        170        180 
FRNRNIIANP NCSTIQMLVA LKPIYDAFGI SRINVATYQS VSGSGKEAIT ELAGQCSKLL 

       190        200        210        220        230        240 
HGLPAESKVY PKQIAFNVLP QIDKFMENGY TKEEMKMVWE TQKIFGDDNI VVNPTAVRVP 

       250        260        270        280        290        300 
VFYGHSEAIH LETIQPAEAE DVKAVLREAP GIELFESNEE YPTAVTESAG TDPVYVGRVR 

       310        320        330 
KDISHSHGIN LWVVSDNIRK GAALNSVQIA EVLIRDYY 

Q56734 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 ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!