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 Q6CBE4

[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_YARLI
Primary accession number Q6CBE4
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 25, 2008 (Entry version 30)
Name and origin of the protein
Protein name Probable trans-2-enoyl-CoA reductase, mitochondrial [Precursor]
Synonym EC 1.3.1.38
Gene name
Name: ETR1
OrderedLocusNames: YALI0C19624g
From
Yarrowia lipolytica (Candida lipolytica) [TaxID: 4952] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CLIB 122 / E 150;
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
CR382129; CAG82338.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_502018.1; -.
3D structure databases
ModBase Q6CBE4.
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:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
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 InterPro).
QuickGo view.
Family and domain databases
InterPro IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
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.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.
ProtoNet Q6CBE4.
Genome annotation databases
GeneID 2909944; -.
KEGG yli:YALI0C19624g; -.
Phylogenomic databases
HOGENOM Q6CBE4; -.
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    12  12     Mitochondrion (Potential). 
CHAIN   13   376  364     Probable trans-2-enoyl-CoA reductase, mitochondrial. PRO_0000000904
Sequence information
Length: 376 AA [This is the length of the unprocessed precursor] Molecular weight: 41206 Da [This is the MW of the unprocessed precursor] CRC64: E085FF7C32379DCB [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLRTLRTSQL ARSGFGTPSF GLRFNSVGRA FVFSQTGEPK DVIQVLEYPI EKPLENQVLL 

        70         80         90        100        110        120 
KSLGFTINPA DINQLEGVYP SVPPKSVQIN NEDAAIGGNE GLFQVLDPGA KSGLKKGDWV 

       130        140        150        160        170        180 
LPRKTCFGTW RSHALVEADT VVKIDNTDLT KVQATTVSVN PSTAYEMLKD LKEGDWFIQN 

       190        200        210        220        230        240 
GGNSGVGRAA IQIGHIRGLK SISVVRDRPD LEVLKKELTD LGATHVITEE EASDKLFSKQ 

       250        260        270        280        290        300 
IKSWTGGKIK LALNCIGGKS ATSIMRQLGA GGSIVTYGGM SKKPLTFPTG PFIFKDITAK 

       310        320        330        340        350        360 
GYWLTRWADK HPEEKAKTIE NIFKFYREKK FVAPPVNIST LDFSKGNDVV LSEFLDALGK 

       370 
AQKGGGKKQL VQWVEY
Q6CBE4 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!