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 O25801

[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_HELPY
Primary accession number O25801
Secondary accession numbers None
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 55)
Name and origin of the protein
Protein name Aspartate-semialdehyde dehydrogenase
Synonyms ASA dehydrogenase
ASADH
EC 1.2.1.11
Gene name
Name: asd
OrderedLocusNames: HP_1189
From
Helicobacter pylori (Campylobacter pylori) [TaxID: 210] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Helicobacteraceae; Helicobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700392 / 26695;
DOI=10.1038/41483; PubMed=9252185 [NCBI, ExPASy, EBI, Israel, Japan]
Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
"The complete genome sequence of the gastric pathogen Helicobacter pylori.";
Nature 388:539-547(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
AE000511; AAD08235.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E64668; E64668.
RefSeq NP_207980.1; -.
3D structure databases
HSSP P00353; 1BRM. [HSSP ENTRY / PDB]
ModBase O25801.
Protein-protein interaction databases
DIP DIP:3753N; -.
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.
Genome annotation databases
GeneID 899951; -.
GenomeReviews AE000511_GR; HP_1189.
KEGG hpy:HP1189; -.
NMPDR fig|85962.1.peg.1176; -.
TIGR HP_1189; -.
Phylogenomic databases
HOGENOM O25801; -.
Other
ProtoNet O25801.
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   346  346     Aspartate-semialdehyde dehydrogenase. PRO_0000141376
ACT_SITE   131   131        Acyl-thioester intermediate (By similarity). 
Sequence information
Length: 346 AA [This is the length of the unprocessed precursor] Molecular weight: 38116 Da [This is the MW of the unprocessed precursor] CRC64: EAF10B9108A72330 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKTYNVAIVG ASGAVGQELI KGLENSFFPI KKFVPLASTR SAGKKIKAFN KDYEILETTH 

        70         80         90        100        110        120 
EVFEREKIDI AFFSAGGSVS EEFATSASKT ALVVDNTSFF RLNKDVPLVV PEINAKEIFN 

       130        140        150        160        170        180 
APLNIIANPN CSTIQMTQIL NPLHLHFKIK SVIVSTYQAV SGAGNKGIES LKNELKTALE 

       190        200        210        220        230        240 
CLEKDPTIDL NQVLQAGAFA YPIAFNAIAH IDTFKENGYT KEELKMLHET HKIMGVDFPI 

       250        260        270        280        290        300 
SATCVRVPVL RSHSESLSIA FEKEFDLKEV YEVLKNAPSV AVCDDPSHNL YPTPLKASHT 

       310        320        330        340 
DSVFIGRLRK DLFDKKTLHG FCVADQLRVG AATNALKIAL HYIKNA
O25801 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 kr flag YPRC Korea Mirror sites: Australia Brazil Canada China Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!