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Q9NKW1 (MFEA_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Peroxisomal multifunctional enzyme A

Short name=MFE-A
Alternative name(s):
MFE-1

Including the following 1 domains:

  1. 3-hydroxyacyl-CoA dehydrogenase
    EC=1.1.1.35
Gene names
Name:mfeA
Synonyms:mfe1
ORF Names:DDB_G0291247
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length441 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Enzyme acting on the peroxisomal beta-oxidation pathway for fatty acids. Protects the cells from the increase of the harmful xenobiotic fatty acids incorporated from their diets and optimizes cellular lipid composition for proper development. Ref.1

Catalytic activity

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subcellular location

Peroxisome Ref.1.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Contains 1 SCP2 domain.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentPeroxisome
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid beta-oxidation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentperoxisome

Traceable author statement PubMed 15225305. Source: dictyBase

   Molecular_function3-hydroxyacyl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

sterol binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 441441Peroxisomal multifunctional enzyme A
PRO_0000328620

Regions

Domain331 – 440110SCP2
Nucleotide binding11 – 3525NAD By similarity
Nucleotide binding73 – 742NAD By similarity
Nucleotide binding162 – 1665NAD By similarity
Nucleotide binding194 – 1974NAD By similarity
Region1 – 3023023-hydroxyacyl-CoA dehydrogenase

Sites

Active site1621Proton acceptor By similarity
Binding site191NAD; via amide nitrogen By similarity
Binding site381NAD By similarity
Binding site971NAD; via carbonyl oxygen By similarity
Binding site1491Substrate By similarity
Binding site4121Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9NKW1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 2CEF3D9779D93BCA

FASTA44146,387
        10         20         30         40         50         60 
MALNFKDKVV IVTGAGGGIG KVYALEFAKR GAKVVVNDLG GSHTGQGSSS KAADKVVEEI 

        70         80         90        100        110        120 
KAAGGTAVAN YDSVEDGEKI VQTAMDSFGG VDILINNAGI LRDVSFGKMT DGDWDLVYRV 

       130        140        150        160        170        180 
HAKGAYKLSR AAWNHMREKN FGRIIMTSSA AGLYGNFGQA NYGSMKMALV GLSNTLAQEG 

       190        200        210        220        230        240 
KSKNIHCNTI APIAASRLTE SVMPPEILEQ MKPDYIVPLV LYLCHQDTTE TGGVFEVGAG 

       250        260        270        280        290        300 
WVSKVRLQRS AGVYMKDLTP EKIKDNWAQI ESFDNPSYPT SASESVSGIL AAVNSKPADG 

       310        320        330        340        350        360 
ESVLVRPPKV AVPKALAATP SGSVVVDGYN ASKIFTTIQG NIGAKGAELV KKINGIYLIN 

       370        380        390        400        410        420 
IKKGTNTQAW ALDLKNGSGS IVVGAGSTKP NVTITVSDED FVDIMTGKLN AQSAFTKGKL 

       430        440 
KISGNMGLAT KLGALMQGSK L 

« Hide

References

« Hide 'large scale' references
[1]"MFE1, a member of the peroxisomal hydroxyacyl coenzyme A dehydrogenase family, affects fatty acid metabolism necessary for morphogenesis in Dictyostelium spp."
Matsuoka S., Saito T., Kuwayama H., Morita N., Ochiai H., Maeda M.
Eukaryot. Cell 2:638-645(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
Strain: AX4.
[2]"The genome of the social amoeba Dictyostelium discoideum."
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. expand/collapse author list , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB042104 mRNA. Translation: BAA94961.1.
AAFI02000177 Genomic DNA. Translation: EAL61607.1.

3D structure databases

ProteinModelPortalQ9NKW1.
SMRQ9NKW1. Positions 3-294.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING44689.DDB_0201628.

Proteomic databases

PRIDEQ9NKW1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0201628; DDB0201628; DDB_G0291247.
KEGGddi:DDB_G0291247.

Organism-specific databases

dictyBaseDDB_G0291247. mfeA.

Phylogenomic databases

eggNOGCOG1028.
OMAHAKGAYK.
PhylomeDBQ9NKW1.
ProtClustDBCLSZ2429570.

Enzyme and pathway databases

UniPathwayUPA00659.

Family and domain databases

Gene3D3.30.1050.10. 1 hit.
3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR003033. SCP2_sterol-bd_dom.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
PF02036. SCP2. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMSSF55718. SSF55718. 1 hit.
ProtoNetSearch...

Other

PROQ9NKW1.

Entry information

Entry nameMFEA_DICDI
AccessionPrimary (citable) accession number: Q9NKW1
Secondary accession number(s): Q54EK5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase