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 O45903


[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 MECR1_CAEEL
Primary accession number O45903
Secondary accession numbers None
Integrated into Swiss-Prot on April 26, 2005
Sequence was last modified on June 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 48)
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
ORFNames: W09H1.5
From
Caenorhabditis elegans [TaxID: 6239] 
Taxonomy Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
DOI=10.1126/science.282.5396.2012; PubMed=9851916 [NCBI, ExPASy, EBI, Israel, Japan]
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for investigating biology.";
Science 282:2012-2018(1998).
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
Z82081; CAB04958.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T26323; T26323.
RefSeq NP_496800.1; -.
UniGene Cel.14175
3D structure databases
HSSP Q8WZM3; 1GU7. [HSSP ENTRY / PDB]
ModBase O45903.
Organism-specific databases
WormBase WBGene00012375; W09H1.5.
WormPep W09H1.5; CE16575. [WormPep / WorfDB]
Gene expression databases
ArrayExpress O45903; -.
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.
Genome annotation databases
Ensembl W09H1.5; Caenorhabditis elegans. [Contig view]
GeneID 174963; -.
KEGG cel:W09H1.5; -.
NMPDR fig|6239.3.peg.7945; -.
Other
NextBio 886210; -.
ProtoNet O45903.
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    14  14     Mitochondrion (Potential). 
CHAIN   15   344  330     Probable trans-2-enoyl-CoA reductase 1, mitochondrial. PRO_0000000892
Sequence information
Length: 344 AA [This is the length of the unprocessed precursor] Molecular weight: 38195 Da [This is the MW of the unprocessed precursor] CRC64: F1E47BB2C89D5268 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLKVLSLRSA LQRAASTRQL VYEGYRNPPE AIQLKTVTIA DKPSADQVLV QWIAAPINPA 

        70         80         90        100        110        120 
DLNQIQGVYP VKPALPAVGG NEGFGKVISV GSNVSSIKVG DHVIPDRSGL GTWRELGLHQ 

       130        140        150        160        170        180 
ENDLFPIDNT LSMEYAATFQ VNPPTAYRML KDFIDLKKGD TVAQNGANSA VGKHVIQICR 

       190        200        210        220        230        240 
ILGIKTVNVV RSRDNLEELV KELKDLGADE VITQEELYSR KKKFPGVKLA LNCVGGRSSL 

       250        260        270        280        290        300 
FLASLLDHGG CMVTYGGMSK QPVDCPTGPL IFKDISLRGF WMSRWYDIQK SPEKRHEMYQ 

       310        320        330        340 
ELAGWMKSGE IKKQEIVKNR LEDHAKALDT ALSKFDKKQF FVLE 

O45903 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!