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 P0C1D9

[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_CORML
Primary accession number P0C1D9
Secondary accession numbers P26511 Q46062
Integrated into Swiss-Prot on May 16, 2006
Sequence was last modified on May 16, 2006 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 17)
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
Corynebacterium melassecola [TaxID: 41643] 
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Corynebacterineae; Corynebacteriaceae; Corynebacterium.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 17965 / AS B-4821;
PubMed=8522535 [NCBI, ExPASy, EBI, Israel, Japan]
Serebrijski I., Wojcik F., Reyes O., Leblon G.;
"Multicopy suppression by asd gene and osmotic stress-dependent complementation by heterologous proA in proA mutants.";
J. Bacteriol. 177:7255-7260(1995).
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
X82928; CAA58101.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S49978; S49978.
3D structure databases
HSSP P00353; 1BRM. [HSSP ENTRY / PDB]
ModBase P0C1D9.
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; 1.
Other
ProtoNet P0C1D9.
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   344  344     Aspartate-semialdehyde dehydrogenase. PRO_0000236032
ACT_SITE   131   131        Acyl-thioester intermediate (By similarity). 
Sequence information
Length: 344 AA [This is the length of the unprocessed precursor] Molecular weight: 36226 Da [This is the MW of the unprocessed precursor] CRC64: 3933583CE88E41F8 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTTIAVVGAT GQVGQVMRTL LEERNFPADT VRFFASPRSA GRKIEFRGTE IEVEDITQAT 

        70         80         90        100        110        120 
EESLKDIDVA LFSAGGTASK QYAPLFAAAG ATVVDNSSAW RKDDEVPLIV SEVNPSDKDS 

       130        140        150        160        170        180 
LVKGIIANPN CTTMAAMPVL KPLHDAAGLV KLHVSSYQAV SGSGLAGVET LAKQVAAVGD 

       190        200        210        220        230        240 
HNVEFVHDGQ AADAGDVGPY VSPIAYNVLP FAGNLVDDGT FETDEEQKLR NESRKILGLP 

       250        260        270        280        290        300 
DLKVSGTCVR VPVFTGHTLT IHAEFDKAIT VEQAQEILGA ASGVKLVDVP TPLAAAGIDE 

       310        320        330        340 
SLVGRIRQDS TVDDNRGLVL VVSGDNLRKG AALNTIQIAE LLVK
P0C1D9 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!