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 Q6BV30


[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 ETR2_DEBHA
Primary accession number Q6BV30
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    November 4, 2008 (Entry version 30)
Name and origin of the protein
Protein name Probable trans-2-enoyl-CoA reductase 2, mitochondrial [Precursor]
Synonym EC 1.3.1.38
Gene name
Name: ETR2
OrderedLocusNames: DEHA0C06545g
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
CR382135; CAG85995.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_457939.1; -.
3D structure databases
SMR Q6BV30; 23-387.
ModBase Q6BV30.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0019166; Molecular function: trans-2-enoyl-CoA reductase (NADPH) activity (inferred from electronic annotation from EC).
GO:0006633; Biological process: fatty acid 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 IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR11695; ADH_Sf_Zn; 1.
Pfam PF08240; ADH_N; 1.
Pfam graphical view of domain structure.
BLOCKS Q6BV30.
ProtoNet Q6BV30.
Genome annotation databases
GeneID 2900740; -.
KEGG dha:DEHA0C06545g; -.
Phylogenomic databases
HOGENOM Q6BV30; -.
Other
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    23  23     Mitochondrion (Potential). 
CHAIN   24   387  364     Probable trans-2-enoyl-CoA reductase 2, mitochondrial. PRO_0000000901
Sequence information
Length: 387 AA [This is the length of the unprocessed precursor] Molecular weight: 42554 Da [This is the MW of the unprocessed precursor] CRC64: 800D3F11D4B64126 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MYRNQLARAS LRSTSSINQI RNMITAQAVV YAQHGEPKDV LKTLKYEIDD DNLDSNSIIV 

        70         80         90        100        110        120 
KTLGSPVNPS DINQIQGVYP SKPEKTTELG SNEPVAVCGN EGLFEILKVG DNVSNFKVGD 

       130        140        150        160        170        180 
WCVPTSVNMG TWRTHMLCGG DEMTKIPNPE QSKANGKPSG LSVNQGATIS VNPLTAYLML 

       190        200        210        220        230        240 
THYVKLTPGK DWFIQNGGNS AVGKYATQIS NLLGINSISV IRDRPDLQDL IKNMTEECGA 

       250        260        270        280        290        300 
TKVITEEQNA SKEFGSEIKS WVKETGGEIK LALNCVGGKN STGIARKLNN NGLMLTYGGM 

       310        320        330        340        350        360 
SMQPVILPTS LHIFKNITSS GFWVTQLLKN DVELKRKTLG QIIEWYENRQ LKDAPSKETK 

       370        380 
FNPSDELSRY YIDGIVNSKG GKQLIVY 

Q6BV30 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!