Q9NKW1 (MFEA_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	441 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Fatty acid metabolism Lipid metabolism
Cellular component	Peroxisome
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid beta-oxidation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	peroxisome Traceable author statement PubMed 15225305. Source: dictyBase
Molecular_function	3-hydroxyacyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro sterol binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 441	441	Peroxisomal multifunctional enzyme A		PRO_0000328620
Regions
	Domain	331 – 440	110	SCP2
	Nucleotide binding	11 – 35	25	NAD By similarity
	Nucleotide binding	73 – 74	2	NAD By similarity
	Nucleotide binding	162 – 166	5	NAD By similarity
	Nucleotide binding	194 – 197	4	NAD By similarity
	Region	1 – 302	302	3-hydroxyacyl-CoA dehydrogenase
Sites
	Active site	162	1	Proton acceptor By similarity
	Binding site	19	1	NAD; via amide nitrogen By similarity
	Binding site	38	1	NAD By similarity
	Binding site	97	1	NAD; via carbonyl oxygen By similarity
	Binding site	149	1	Substrate By similarity
	Binding site	412	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9NKW1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 2CEF3D9779D93BCA	FASTA	441	46,387
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
RefSeq	XP_635235.1. XM_630143.1.
3D structure databases
HSSP	HSSP built from PDB template 2ET6 based on UniProtKB P22414.
ProteinModelPortal	Q9NKW1.
SMR	Q9NKW1. Positions 3-294.
ModBase	Search...
Protein-protein interaction databases
STRING	44689.DDB_0201628.
Proteomic databases
PRIDE	Q9NKW1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0201628; DDB0201628; DDB_G0291247.
GeneID	8628181.
KEGG	ddi:DDB_G0291247.
Organism-specific databases
dictyBase	DDB_G0291247. mfeA.
Phylogenomic databases
eggNOG	COG1028.
OMA	HAKGAYK.
ProtClustDB	CLSZ2429570.
Enzyme and pathway databases
UniPathway	UPA00659.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. IPR003033. SCP2_sterol-bd_dom. [Graphical view]
Pfam	PF00106. adh_short. 1 hit. PF02036. SCP2. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
SUPFAM	SSF55718. SCP2. 1 hit.
PROSITE	PS00061. ADH_SHORT. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MFEA_DICDI

Accession

Primary (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:	May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)