(data stored in ACNUC7421 zone)

HOGENOM: ARATH_3_PE875

ID   ARATH_3_PE875                        STANDARD;      PRT;   725 AA.
AC   ARATH_3_PE875; Q9ZPI5;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Peroxisomal fatty acid beta-oxidation multifunctional
DE   protein MFP2; Short=AtMPF2;Includes: RecName: Full=Enoyl-CoA
DE   hydratase/3-2-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase;
DE   EC=4.2.1.17; EC=5.1.2.3; EC=5.3.3.8;Includes: RecName:
DE   Full=3-hydroxyacyl-CoA dehydrogenase; EC=1.1.1 35; (ARATH_3.PE875).
GN   Name=MFP2; OrderedLocusNames=At3g06860; ORFNames=F17A9.1;
OS   ARABIDOPSIS THALIANA.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; rosids;
OC   eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ARATH_3.PE875.
CC       Arabidopsis thaliana chromosome 3 TAIR10 full sequence 1..23459830
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:MFP2_ARATH
CC   -!- FUNCTION: Involved in peroxisomal fatty acid beta-oxidation during
CC       seed germination. Possesses enoyl-CoA hydratase activity against
CC       long chain substrates (C14-C18) and 3-hydroxyacyl-CoA
CC       dehydrogenase activity against chains of variable sizes (C6-C18).
CC   -!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-
CC       CoA + H(2)O.
CC   -!- CATALYTIC ACTIVITY: (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-
CC       CoA.
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxybutanoyl-CoA = (R)-3-
CC       hydroxybutanoyl-CoA.
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
CC       + NADH.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=240 uM for crotonyl-CoA;
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC   -!- SUBCELLULAR LOCATION: Glyoxysome (Probable). Peroxisome
CC       (Probable).
CC   -!- TISSUE SPECIFICITY: Highly expressed in senescing leaves and at
CC       lower levels in flowers and siliques.
CC   -!- DEVELOPMENTAL STAGE: Expression increases rapidly during seed
CC       germination to reach a peak at 2-3 days after imbibition (DAI) and
CC       then declines to basal levels at 5 DAI.
CC   -!- DOMAIN: The epimerase and isomerase activities are contained in
CC       the N-terminal region while the dehydrogenase activity is in the
CC       C-terminal region (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Accumulation of long-chain acyl-CoA
CC       substrates and increased size of peroxisomes.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family.
CC   -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-
CC       CoA dehydrogenase family.
CC   -!- GENE_FAMILY: HOG000261347 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Arabidopsis_thaliana;AT3G06860;AT3G06860.1;AT3G06860.1.
DR   EMBL; AC016827; - ;
DR   EMBL; AF123254; - ;
DR   EMBL; AY062621; - ;
DR   EMBL; AY062650; - ;
DR   UniProtKB/Swiss-Prot; Q9ZPI5; -.
DR   EMBL; AF123254; AAD18042.1; -; mRNA.
DR   EMBL; AC016827; AAF26990.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74468.1; -; Genomic_DNA.
DR   EMBL; AY062621; AAL32699.1; -; mRNA.
DR   IPI; IPI00520365; -.
DR   RefSeq; NP_187342.1; NM_111566.3.
DR   UniGene; At.24386; -.
DR   PDB; 2WTB; X-ray; 2.50 A; A=1-725.
DR   PDBsum; 2WTB; -.
DR   ProteinModelPortal; Q9ZPI5; -.
DR   SMR; Q9ZPI5; 7-719.
DR   STRING; Q9ZPI5; -.
DR   PRIDE; Q9ZPI5; -.
DR   ProMEX; Q9ZPI5; -.
DR   EnsemblPlants; AT3G06860.1; AT3G06860.1; AT3G06860.
DR   GeneID; 819870; -.
DR   GenomeReviews; BA000014_GR; AT3G06860.
DR   KEGG; ath:AT3G06860; -.
DR   NMPDR; fig|3702.1.peg.12706; -.
DR   TAIR; At3g06860; -.
DR   GeneTree; EPGT00070000028643; -.
DR   InParanoid; Q9ZPI5; -.
DR   OMA; GYISIDI; -.
DR   PhylomeDB; Q9ZPI5; -.
DR   ProtClustDB; CLSN2684794; -.
DR   Genevestigator; Q9ZPI5; -.
DR   GO; GO:0005618; C:cell wall; IDA:TAIR.
DR   GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:EC.
DR   GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
DR   GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:EC.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:EC.
DR   GO; GO:0016508; F:long-chain-enoyl-CoA hydratase activity; IDA:UniProtKB.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEP:TAIR.
DR   InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
DR   InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR   InterPro; IPR006108; 3HC_DH_C.
DR   InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR   InterPro; IPR001753; Crotonase_core.
DR   InterPro; IPR013328; DH_multihelical.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:1.10.1040.10; Opine_DH; 2.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH; 1.
DR   SUPFAM; SSF48179; 6DGDH_C_like; 2.
DR   PROSITE; PS00067; 3HCDH; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
DR   HOGENOMDNA; ARATH_3.PE875; -.
KW   AT3G06860pg.C_scaffold_1320000031; AT3G06860.1.C_scaffold_1320000031;
KW   Q8W4D2; AC016827; AF123254; AY062621; AY062650;
KW   3D-structure; Complete proteome; Fatty acid metabolism; Glyoxysome;
KW   Isomerase; Lipid metabolism; Lyase; Multifunctional enzyme; NAD;
KW   Oxidoreductase; Peroxisome; Reference proteome.
SQ   SEQUENCE   725 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDSRTKGKTV MEVGGDGVAV ITLINPPVNS LSFDVLYNLK SNYEEALSRN DVKAIVITGA
     KGRFSGGFDI SGFGEMQKGN VKEPKAGYIS IDIITDLLEA ARKPSVAAID GLALGGGLEL
     AMACHARISA PAAQLGLPEL QLGVIPGFGG TQRLPRLVGL TKALEMILTS KPVKAEEGHS
     LGLIDAVVPP AELVTTARRW ALDIVGRRKP WVSSVSKTDK LPPLGEAREI LTFAKAQTLK
     RAPNMKHPLM CLDAIEVGIV SGPRAGLEKE AEVASQVVKL DTTKGLIHVF FSQRGTAKVP
     GVTDRGLVPR KIKKVAIIGG GLMGSGIATA LILSNYPVIL KEVNEKFLEA GIGRVKANLQ
     SRVRKGSMSQ EKFEKTMSLL KGSLDYESFR DVDMVIEAVI ENISLKQQIF ADLEKYCPQH
     CILASNTSTI DLNKIGERTK SQDRIVGAHF FSPAHIMPLL EIVRTNHTSA QVIVDLLDVG
     KKIKKTPVVV GNCTGFAVNR MFFPYTQAAM FLVECGADPY LIDRAISKFG MPMGPFRLCD
     LVGFGVAIAT ATQFIENFSE RTYKSMIIPL MQEDKRAGEA TRKGFYLYDD KRKAKPDPEL
     KKYIEKARSI SGVKLDPKLA NLSEKDIIEM TFFPVVNEAC RVFAEGIAVK AADLDIAGIM
     GMGFPPYRGG IMFWADSIGS KYIYSRLDEW SKAYGEFFKP CAFLAERGSK GVLLSAPVKQ
     ASSRL
//

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