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 P96198

[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_AZOVI
Primary accession number P96198
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on May 1, 1997 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 44)
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
Azotobacter vinelandii [TaxID: 354] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Azotobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW;
DOI=10.1007/s004380050409; PubMed=9108283 [NCBI, ExPASy, EBI, Israel, Japan]
Manna A.C., Das H.K.;
"Characterization and mutagenesis of the leucine biosynthetic genes of Azotobacter vinelandii: an analysis of the rarity of amino acid auxotrophs.";
Mol. Gen. Genet. 254:207-217(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
Y11280; CAA72152.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P00353; 1BRM. [HSSP ENTRY / PDB]
ModBase P96198.
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 P96198.
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   368  368     Aspartate-semialdehyde dehydrogenase. PRO_0000141360
ACT_SITE   134   134        Acyl-thioester intermediate (By similarity). 
Sequence information
Length: 368 AA [This is the length of the unprocessed precursor] Molecular weight: 40388 Da [This is the MW of the unprocessed precursor] CRC64: 0F9B62D790C0AAD5 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKRVGLIGWR GMVGSVLMQR MLEERDFDLI EPVFFTTSSV GGQGAIGKET VPLKDAYSIE 

        70         80         90        100        110        120 
ELKSLDAIIT CQGGDYTSEV FPKLRDAGWQ GYWIDAASSL RMADDAVIVL DPVNRRVIDQ 

       130        140        150        160        170        180 
SLDAGVKNYI GGNCTVSLML MALGRLRGRP GRLDERHDLS GRFRAGAQNM RELIRQMGTI 

       190        200        210        220        230        240 
NAAVAAEPAD PASAILEIDR KGPETQRSAE FPVDHFGVPL AGSLIPYIDK ELPNGQSREE 

       250        260        270        280        290        300 
WKGQAETNKI LGRIKNPIPV DGICVRVGAM RCHSQALTIK LNKDVPIADI EGLISQHNPW 

       310        320        330        340        350        360 
VKLVPNHREA SMQELSPAAI TGTLTVPVGR LRKLNMGSQY LGAFTVGDQL LWGAAEPVRR 


MLLILLER
P96198 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 ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!