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UniProtKB/Swiss-Prot entry Q89AB8

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

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Entry information
Entry name DHAS_BUCBP
Primary accession number Q89AB8
Secondary accession numbers None
Integrated into Swiss-Prot on November 14, 2003
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 39)
Name and origin of the protein
Protein name Aspartate-semialdehyde dehydrogenase
Synonyms ASA dehydrogenase
EC 1.2.1.11
Gene name
Name: asd
OrderedLocusNames: bbp_398
From
Buchnera aphidicola subsp. Baizongia pistaciae [TaxID: 135842] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0235981100; PubMed=12522265 [NCBI, ExPASy, EBI, Israel, Japan]
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
"Reductive genome evolution in Buchnera aphidicola.";
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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
AE016826; AAO27110.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_778005.1; -.
3D structure databases
HSSP P00353; 1BRM. [HSSP ENTRY / PDB]
ModBase Q89AB8.
Enzyme and pathway databases
BioCyc BAPH224915:BBP_398-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.
BLOCKS Q89AB8.
ProtoNet Q89AB8.
Genome annotation databases
GeneID 1058293; -.
GenomeReviews AE016826_GR; bbp_398.
KEGG bab:bbp398; -.
Phylogenomic databases
HOGENOM Q89AB8; -.
Genome annotation databases
CMR Q89AB8; bbp_398.
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   369  369     Aspartate-semialdehyde dehydrogenase. PRO_0000141365
ACT_SITE   137   137        Acyl-thioester intermediate (By similarity). 
Sequence information
Length: 369 AA [This is the length of the unprocessed precursor] Molecular weight: 41494 Da [This is the MW of the unprocessed precursor] CRC64: 8DDBA2BADF6C7516 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKKNIGLIGW RGMVGSVLVE RMICENDFFH FNPIFFSTSQ KNSKGPTING EYFGVLKDAY 

        70         80         90        100        110        120 
DLDILKELDI LISCQGSDYT NKVYFKLRDI GWNGYWIDAA SVLRMNQDTV IILDPVNSNT 

       130        140        150        160        170        180 
IRESIDSGFK TFVGGNCTVS LMLMSLGGLF SEKLIEWITV STYQAASGSG AKYIEELLMQ 

       190        200        210        220        230        240 
MGSMYTEASG YLGNPAHSIL NIEKKVRNLS CSDKFPKKNF KVPLAGSLIP WIDKKMRNGQ 

       250        260        270        280        290        300 
SREEWKIQAE TNKILSSNKD ILIDGLCVRI GALRCHSQSF VIKLKKDISI PEIEQILLNH 

       310        320        330        340        350        360 
NSWTKVIPNR KHDTMTELTP AAVTGTLNTP VGRLRKLNIG QKYLSAFTVG DQLLWGASEP 


LRRMLKFLI
Q89AB8 in FASTA format

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