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 Q6BLV6


[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 ETR1_DEBHA
Primary accession number Q6BLV6
Secondary accession numbers None
Integrated into Swiss-Prot on April 26, 2005
Sequence was last modified on August 16, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 26)
Name and origin of the protein
Protein name Probable trans-2-enoyl-CoA reductase 1, mitochondrial [Precursor]
Synonym EC 1.3.1.38
Gene name
Name: ETR1
OrderedLocusNames: DEHA0F11319g
From
Debaryomyces hansenii (Yeast) (Torulaspora hansenii) [TaxID: 4959] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Debaryomyces.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 36239 / CBS 767 / IFO 0083 / IGC 2968 / JCM 1990;
DOI=10.1038/nature02579; PubMed=15229592 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
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
CR382138; CAG89156.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_460815.1; -.
3D structure databases
ModBase Q6BLV6.
Ontologies
GO
GO:0019166; Molecular function: trans-2-enoyl-CoA reductase (NADPH) activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
Graphical view of domain structure.
PANTHER PTHR11695; ADH_Sf_Zn; 1.
Pfam PF08240; ADH_N; 1.
Pfam graphical view of domain structure.
BLOCKS Q6BLV6.
Genome annotation databases
GeneID 2904327; -.
KEGG dha:DEHA0F11319g; -.
Phylogenomic databases
HOGENOM Q6BLV6; -.
Other
ProtoNet Q6BLV6.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Fatty acid biosynthesis; Lipid synthesis; Mitochondrion; NADP; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
TRANSIT   1     ?        Mitochondrion (Potential). 
CHAIN   ?   378        Probable trans-2-enoyl-CoA reductase 1, mitochondrial. PRO_0000000900
Sequence information
Length: 378 AA [This is the length of the unprocessed precursor] Molecular weight: 41243 Da [This is the MW of the unprocessed precursor] CRC64: CA83C11C8D31FB2F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVKINASAIT YTKGGEISKI LLGTGFSIDT ETLGPKQVVI QALATPINPS DLNQLAGTYA 

        70         80         90        100        110        120 
SKPNFTSELD TPVPVAIGGN EGLYKVIEVG SDVTSYKNGD WVIPKMPSFG TWRTHALVTL 

       130        140        150        160        170        180 
DKPENPDPFI KVSSEDDKSI DLTQAATVSI NPSTAYQLID QFIKDWDPKG NDWIIQNGGN 

       190        200        210        220        230        240 
SQVGKFVVQI AKIRNIKTIS VIRDGKPDQD QIVKELLDLG ATKVITDKEA ESEEYINKIV 

       250        260        270        280        290        300 
PGWVNEGKVI LALNCVCGKS GSALVSHLTG NHLADYRSPH LVTYGGMLGQ PLMYSSSESL 

       310        320        330        340        350        360 
FKNVTSKAYW LTANTKRNPQ SKVDTVKKVL ALYKSGDIKP VPFNGKEFNI KSTSDDYIKL 

       370 
FLRGIAESKT GKQVIVYN 

Q6BLV6 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 ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!