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 Q41247


[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 AL7A1_BRANA
Primary accession number Q41247
Secondary accession numbers None
Integrated into Swiss-Prot on November 15, 2002
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 52)
Name and origin of the protein
Protein name Aldehyde dehydrogenase family 7 member A1
Synonyms EC 1.2.1.3
Antiquitin-1
Brassica turgor-responsive/drought-induced gene 26 protein
Btg-26
Gene name
Name: BTG-26
From
Brassica napus (Rape) [TaxID: 3708] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Brassica.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
STRAIN=cv. Bridger;
TISSUE=Leaf;
DOI=10.1007/BF00019320; PubMed=7894018 [NCBI, ExPASy, EBI, Israel, Japan]
Stroeher V.L., Boothe J.G., Good A.G.;
"Molecular cloning and expression of a turgor-responsive gene in Brassica napus.";
Plant Mol. Biol. 27:541-551(1995).
[2]
PROTEIN SEQUENCE OF 2-16.
DOI=10.1016/S0014-5793(02)02553-X; PubMed=11959129 [NCBI, ExPASy, EBI, Israel, Japan]
Tang W.-K., Cheng C.H.K., Fong W.-P.;
"First purification of the antiquitin protein and demonstration of its enzymatic activity.";
FEBS Lett. 516:183-186(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
S77096; AAB33843.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S53503; S53503.
3D structure databases
HSSP P05091; 1O04. [HSSP ENTRY / PDB]
ModBase Q41247.
Ontologies
GO
GO:0004029; Molecular function: aldehyde dehydrogenase (NAD) activity (non-traceable author statement from UniProtKB).
GO:0006081; Biological process: cellular aldehyde metabolic process (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
PANTHER PTHR11699; Aldehyde_dehyd; 1.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
PROSITE PS00687; ALDEHYDE_DEHYDR_GLU; 1.
BLOCKS Q41247.
Other
ProtoNet Q41247.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Direct protein sequencing; NAD; Oxidoreductase; Stress response.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   494  493     Aldehyde dehydrogenase family 7 member A1. PRO_0000056496
NP_BIND   247   252  6     NAD (By similarity). 
ACT_SITE   269   269        Proton acceptor (By similarity). 
ACT_SITE   303   303        Nucleophile (By similarity). 
SITE   168   168  1     Transition state stabilizer (By similarity). 
Sequence information
Length: 494 AA [This is the length of the unprocessed precursor] Molecular weight: 52688 Da [This is the MW of the unprocessed precursor] CRC64: 13ED0096563BAE13 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGSASKEYEF LSEIGLSSSH NLGNYVGGKW LGNGPLVSTL NPANNQVLPI AQVVEASLED 

        70         80         90        100        110        120 
YEIGLKACEE AAKTWMQVPA PKRGDIVRQI GDALRSKLDY LGRLLSLEMG KILAEGIGEV 

       130        140        150        160        170        180 
QEVIDMCDFA VGLSRQLNGS VIPSERPNHM MLEMWNPLGI VGVITAFNFP CAVLGWNACI 

       190        200        210        220        230        240 
ALVCGNCVVW KGAPTTPLIT IAMTKLVAEV LEKNHLPGAI FTAMCGGAEI GEAIAKDTRI 

       250        260        270        280        290        300 
PLVSFTGSSK VGLTVQQTVS ARSGKTLLEL SGNNAIIVMD DADIQLAARS VLFAAVGTAG 

       310        320        330        340        350        360 
QRCTTCRRLL LHESVYDKVL EQLLTSYKQV KIGDPLEKGT LLGPLHTPES KKNFEKGIEV 

       370        380        390        400        410        420 
IKSQGGKVLT GGKAVEGEGN FVEPTIIEIS SDAAVVKEEL FAPVLYALKF KTFEEAVAIN 

       430        440        450        460        470        480 
NSVPQGLSSS IFTRSPDNIF KWIGPMGSDC GIVNVNIPTN GAEIGGAFGG EKATGGGREA 

       490 
GSDSWKQYMR RSTW 

Q41247 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!