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 Q5EU90


[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 TER_EUGGR
Primary accession number Q5EU90
Secondary accession numbers None
Integrated into Swiss-Prot on March 29, 2005
Sequence was last modified on March 15, 2005 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 15)
Name and origin of the protein
Protein name Trans-2-enoyl-CoA reductase, mitochondrial [Precursor]
Synonym EC 1.3.1.44
Gene name
Name: TER
From
Euglena gracilis [TaxID: 3039] 
Taxonomy Eukaryota; Euglenozoa; Euglenida; Euglenales; Euglena.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], BLOCKAGE OF N-TERMINUS, IDENTIFICATION BY MASS SPECTROMETRY, ENZYME ACTIVITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
STRAIN=SAG 1224-5/25;
DOI=10.1074/jbc.M411010200; PubMed=15569691 [NCBI, ExPASy, EBI, Israel, Japan]
Hoffmeister M., Piotrowski M., Nowitzki U., Martin W.;
"Mitochondrial trans-2-enoyl-CoA reductase of wax ester fermentation from Euglena gracilis defines a new family of enzymes involved in lipid synthesis.";
J. Biol. Chem. 280:4329-4338(2005).
Comments
  • FUNCTION: Catalyzes reduction of enoyl-CoA to acyl-CoA, an important step of fatty acid biosynthesis which is performed under anaerobiosis. Under anaeobiosis, mitochondria perform a malonyl-CoA independent synthesis of fatty acids leading to accumulation of wax esters, which serve as the sink for electrons stemming from glycolytic ATP synthesis and pyruvate oxidation. Can use both NADH and NADPH as electron donor, with 2-3-fold higher specific activities for NADH relative to NADPH.
  • CATALYTIC ACTIVITY: Acyl-CoA + NAD+ = trans-didehydroacyl-CoA + NADH.
  • BIOPHYSICOCHEMICAL PROPERTIES:
    Kinetic parameters:   KM=68 µM for NADH;
    KM=119 µM for NADPH;
    KM=91 µM for trans-2-hexenoyl-CoA;
  • SUBUNIT: Monomer.
  • SUBCELLULAR LOCATION: Mitochondrion.
  • DEVELOPMENTAL STAGE: Expressed under aerobic and anaerobic conditions.
  • PTM: The N-terminus is blocked.
  • SIMILARITY: Belongs to the TER reductase family.
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
AY741582; AAW66853.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
ModBase Q5EU90.
Family and domain databases
InterPro IPR010758; AlcDHase_sc.
Graphical view of domain structure.
Pfam PF07055; scADH; 1.
Pfam graphical view of domain structure.
BLOCKS Q5EU90.
Other
ProtoNet Q5EU90.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Mitochondrion; NAD; NADP; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
TRANSIT   1    68  68     Mitochondrion (By similarity). 
CHAIN   69   539  471     Trans-2-enoyl-CoA reductase, mitochondrial. PRO_0000033619
Sequence information
Length: 539 AA [This is the length of the unprocessed precursor] Molecular weight: 57303 Da [This is the MW of the unprocessed precursor] CRC64: A52C244AC61E2CDF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSCPASPSAA VVSAGALCLC VATVLLATGS NPTALSTAST RSPTSLVRGV DRGLMRPTTA 

        70         80         90        100        110        120 
AALTTMREVP QMAEGFSGEA TSAWAAAGPQ WAAPLVAAAS SALALWWWAA RRSVRRPLAA 

       130        140        150        160        170        180 
LAELPTAVTH LAPPMAMFTT TAKVIQPKIR GFICTTTHPI GCEKRVQEEI AYARAHPPTS 

       190        200        210        220        230        240 
PGPKRVLVIG CSTGYGLSTR ITAAFGYQAA TLGVFLAGPP TKGRPAAAGW YNTVAFEKAA 

       250        260        270        280        290        300 
LEAGLYARSL NGDAFDSTTK ARTVEAIKRD LGTVDLVVYS IAAPKRTDPA TGVLHKACLK 

       310        320        330        340        350        360 
PIGATYTNRT VNTDKAEVTD VSIEPASPEE IADTVKVMGG EDWELWIQAL SEAGVLAEGA 

       370        380        390        400        410        420 
KTVAYSYIGP EMTWPVYWSG TIGEAKKDVE KAAKRITQQY GCPAYPVVAK ALVTQASSAI 

       430        440        450        460        470        480 
PVVPLYICLL YRVMKEKGTH EGCIEQMVRL LTTKLYPENG APIVDEAGRV RVDDWEMAED 

       490        500        510        520        530 
VQQAVKDLWS QVSTANLKDI SDFAGYQTEF LRLFGFGIDG VDYDQPVDVE ADLPSAAQQ 

Q5EU90 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!