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UniProtKB/Swiss-Prot entry Q8K9B5

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

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Entry information
Entry name DHAS_BUCAP
Primary accession number Q8K9B5
Secondary accession numbers None
Integrated into Swiss-Prot on November 8, 2002
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 42)
Name and origin of the protein
Protein name Aspartate-semialdehyde dehydrogenase
Synonyms ASA dehydrogenase
EC 1.2.1.11
Gene name
Name: asd
OrderedLocusNames: BUsg_433
From
Buchnera aphidicola subsp. Schizaphis graminum [TaxID: 98794] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan]
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
"50 million years of genomic stasis in endosymbiotic bacteria.";
Science 296:2376-2379(2002).
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
AE013218; AAM67976.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_660765.1; -.
3D structure databases
HSSP P00353; 1BRM. [HSSP ENTRY / PDB]
ModBase Q8K9B5.
Enzyme and pathway databases
BioCyc BAPH198804:BUSG433-MON; -.
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.
ProtoNet Q8K9B5.
Genome annotation databases
GeneID 1005553; -.
GenomeReviews AE013218_GR; BUsg_433.
KEGG bas:BUsg433; -.
Phylogenomic databases
HOGENOM Q8K9B5; -.
Genome annotation databases
CMR Q8K9B5; BUsg_433.
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
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   371  371     Aspartate-semialdehyde dehydrogenase. PRO_0000141364
ACT_SITE   137   137        Acyl-thioester intermediate (By similarity). 
Sequence information
Length: 371 AA [This is the length of the unprocessed precursor] Molecular weight: 41785 Da [This is the MW of the unprocessed precursor] CRC64: 079A0E1BEAE68318 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTKSVGIIGW RGMVGSVLLK RMQEENDFSK IIPYFFSTSQ SGQDGPIINN ILSKNLKDAY 

        70         80         90        100        110        120 
NINLLQEMDI IITCQGSSYT EKIYPKLRNN NWQGYWIDAA STLRMEKDAT IILDPVNLNV 

       130        140        150        160        170        180 
INNALDKGIK TFVGGNCTVS LMLMALGGLF VNNLIDWVFV STYQAASGAG SRYVIELLKQ 

       190        200        210        220        230        240 
MGSLYNVVSK DLLDKSYSVL DIEKKVTQES RSKNFPLENF SVPLATSLIP WIDVEMKNGQ 

       250        260        270        280        290        300 
SREEWKGQAE TNKILNLKKK VLIDGTCVRI SSIRCHSQSF LIKLNKDISL ENIKKIIVNH 

       310        320        330        340        350        360 
NQWVDVIPNN MQKTLCNLTP SAVTDTLNIP IGRLRKLNID DRYLSAFTVG DQLLWGAAEP 

       370 
LRRMLNLLVN I
Q8K9B5 in FASTA format

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