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Q9XXC8 (MECR2_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable trans-2-enoyl-CoA reductase 2, mitochondrial

EC=1.3.1.38
Gene names
ORF Names:Y48A6B.9
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Oxidoreductase with a preference for short and medium chain substrates, including trans-2-hexenoyl-CoA (C6), trans-2-decenoyl-CoA (C10), and trans-2-hexadecenoyl-CoA (C16). May play a role in mitochondrial fatty acid synthesis By similarity.

Catalytic activity

Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiontrans-2-enoyl-CoA reductase (NADPH) activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2222Mitochondrion Potential
Chain23 – 346324Probable trans-2-enoyl-CoA reductase 2, mitochondrial
PRO_0000000893

Regions

Nucleotide binding157 – 1604NADP By similarity
Nucleotide binding180 – 1823NADP By similarity
Nucleotide binding249 – 2524NADP By similarity

Sites

Binding site1311NADP By similarity
Binding site3321NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9XXC8 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: E14426AADA5FB4A6

FASTA34637,944
        10         20         30         40         50         60 
MQKTIRSQAL IYRKFGDPLK VLQLETVEVP AEPGSGECLV EWLASPINPL DINRIQGNYA 

        70         80         90        100        110        120 
VRAELPVIGG SEGVGRVVKA GSGSRFKSGD HVTIFSANTP IWTEFGVVDD DELVKLDNRI 

       130        140        150        160        170        180 
PLDLAATLMI NPPTAWIMLK KYVNLQKGDY IIQNSANSGV GRSVIEMCKA LGYKSINIVR 

       190        200        210        220        230        240 
NRQNIEALKT DLWRIGADHV FTEEEFKGTS RQFLKSINVR PKLALNGVGG KSALQISSVL 

       250        260        270        280        290        300 
ERGGTCVTYG GMSKKAHEFT TSALVFNDIC VRGVAVGMWA RQEEHLDEWN LCVDEVQKLA 

       310        320        330        340 
VAGKITAIPM EKVVLADHKT AIQKSLEGRS IKQLFVINSK ASASHI 

« Hide

References

[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL023844 Genomic DNA. Translation: CAA19533.1.
PIRT26986.
RefSeqNP_001255097.1. NM_001268168.1.
UniGeneCel.9759.

3D structure databases

ProteinModelPortalQ9XXC8.
SMRQ9XXC8. Positions 6-329.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid41720. 1 interaction.
DIPDIP-24981N.
IntActQ9XXC8. 2 interactions.
MINTMINT-1059728.
STRING6239.Y48A6B.9.

Proteomic databases

PaxDbQ9XXC8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaY48A6B.9a; Y48A6B.9a; WBGene00012970.
GeneID176534.
KEGGcel:CELE_Y48A6B.9.
UCSCY48A6B.9. c. elegans.

Organism-specific databases

CTD176534.
WormBaseY48A6B.9a; CE19192; WBGene00012970.

Phylogenomic databases

eggNOGCOG0604.
GeneTreeENSGT00740000115589.
HOGENOMHOG000294683.
InParanoidQ9XXC8.
KOK07512.
OMASANTPIW.
PhylomeDBQ9XXC8.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11695. PTHR11695. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. SSF50129. 1 hit.
ProtoNetSearch...

Other

NextBio892980.

Entry information

Entry nameMECR2_CAEEL
AccessionPrimary (citable) accession number: Q9XXC8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: November 1, 1999
Last modified: June 11, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase