MFEA_DICDI
ID MFEA_DICDI Reviewed; 441 AA.
AC Q9NKW1; Q54EK5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Peroxisomal multifunctional enzyme A;
DE Short=MFE-A;
DE AltName: Full=MFE-1;
DE Includes:
DE RecName: Full=3-hydroxyacyl-CoA dehydrogenase;
DE EC=1.1.1.35;
GN Name=mfeA; Synonyms=mfe1; ORFNames=DDB_G0291247;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=AX4;
RX PubMed=12796309; DOI=10.1128/ec.2.3.638-645.2003;
RA Matsuoka S., Saito T., Kuwayama H., Morita N., Ochiai H., Maeda M.;
RT "MFE1, a member of the peroxisomal hydroxyacyl coenzyme A dehydrogenase
RT family, affects fatty acid metabolism necessary for morphogenesis in
RT Dictyostelium spp.";
RL Eukaryot. Cell 2:638-645(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Enzyme acting on the peroxisomal beta-oxidation pathway for
CC fatty acids. Protects the cells from the increase of the harmful
CC xenobiotic fatty acids incorporated from their diets and optimizes
CC cellular lipid composition for proper development.
CC {ECO:0000269|PubMed:12796309}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:12796309}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AB042104; BAA94961.1; -; mRNA.
DR EMBL; AAFI02000177; EAL61607.1; -; Genomic_DNA.
DR RefSeq; XP_635235.1; XM_630143.1.
DR AlphaFoldDB; Q9NKW1; -.
DR SMR; Q9NKW1; -.
DR STRING; 44689.DDB0201628; -.
DR PaxDb; Q9NKW1; -.
DR EnsemblProtists; EAL61607; EAL61607; DDB_G0291247.
DR GeneID; 8628181; -.
DR KEGG; ddi:DDB_G0291247; -.
DR dictyBase; DDB_G0291247; mfeA.
DR eggNOG; ENOG502QPX4; Eukaryota.
DR HOGENOM; CLU_010194_14_2_1; -.
DR InParanoid; Q9NKW1; -.
DR OMA; ECLPYLQ; -.
DR PhylomeDB; Q9NKW1; -.
DR UniPathway; UPA00659; -.
DR PRO; PR:Q9NKW1; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005777; C:peroxisome; IDA:dictyBase.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0140582; P:adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway; IMP:dictyBase.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR GO; GO:0006631; P:fatty acid metabolic process; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR Gene3D; 3.30.1050.10; -; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003033; SCP2_sterol-bd_dom.
DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF02036; SCP2; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF55718; SSF55718; 1.
PE 2: Evidence at transcript level;
KW Fatty acid metabolism; Lipid metabolism; NAD; Oxidoreductase; Peroxisome;
KW Reference proteome.
FT CHAIN 1..441
FT /note="Peroxisomal multifunctional enzyme A"
FT /id="PRO_0000328620"
FT DOMAIN 331..440
FT /note="SCP2"
FT REGION 1..302
FT /note="3-hydroxyacyl-CoA dehydrogenase"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 11..35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 73..74
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 162..166
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 194..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 441 AA; 46387 MW; 2CEF3D9779D93BCA CRC64;
MALNFKDKVV IVTGAGGGIG KVYALEFAKR GAKVVVNDLG GSHTGQGSSS KAADKVVEEI
KAAGGTAVAN YDSVEDGEKI VQTAMDSFGG VDILINNAGI LRDVSFGKMT DGDWDLVYRV
HAKGAYKLSR AAWNHMREKN FGRIIMTSSA AGLYGNFGQA NYGSMKMALV GLSNTLAQEG
KSKNIHCNTI APIAASRLTE SVMPPEILEQ MKPDYIVPLV LYLCHQDTTE TGGVFEVGAG
WVSKVRLQRS AGVYMKDLTP EKIKDNWAQI ESFDNPSYPT SASESVSGIL AAVNSKPADG
ESVLVRPPKV AVPKALAATP SGSVVVDGYN ASKIFTTIQG NIGAKGAELV KKINGIYLIN
IKKGTNTQAW ALDLKNGSGS IVVGAGSTKP NVTITVSDED FVDIMTGKLN AQSAFTKGKL
KISGNMGLAT KLGALMQGSK L
