ID   MFP_ORYSJ               Reviewed;         726 AA.
AC   Q8W1L6; Q0E238; Q336K1; Q6K7T9;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Peroxisomal fatty acid beta-oxidation multifunctional protein;
DE            Short=MFP;
DE   Includes:
DE     RecName: Full=Enoyl-CoA hydratase/3-2-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase;
DE              EC=4.2.1.17;
DE              EC=5.1.2.3;
DE              EC=5.3.3.8;
DE   Includes:
DE     RecName: Full=3-hydroxyacyl-CoA dehydrogenase;
DE              EC=1.1.1.35;
GN   Name=MFP; OrderedLocusNames=Os02g0274100, LOC_Os02g17390;
GN   ORFNames=P0413A11.18;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, RNA-BINDING,
RP   MICROTUBULE-BINDING, AND CATALYTIC ACTIVITY.
RC   TISSUE=Seed {ECO:0000269|PubMed:11706039};
RX   PubMed=11706039; DOI=10.1074/jbc.m109510200;
RA   Chuong S.D.X., Mullen R.T., Muench D.G.;
RT   "Identification of a rice RNA- and microtubule-binding protein as the
RT   multifunctional protein, a peroxisomal enzyme involved in the beta-
RT   oxidation of fatty acids.";
RL   J. Biol. Chem. 277:2419-2429(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 7-726.
RA   Gaur R., Tyagi A.K.;
RT   "Isolation and characterization of a multi-functional protein (OsMFP) gene
RT   from rice.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Multifunctional enzyme involved in fatty acid beta-oxidation.
CC       Also binds to RNA and microtubules. Possible role in subcellular mRNA
CC       localization and RNA-cytoskeleton interactions.
CC       {ECO:0000269|PubMed:11706039, ECO:0000303|PubMed:11706039}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:58856; EC=4.2.1.17;
CC         Evidence={ECO:0000269|PubMed:11706039};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC         ChEBI:CHEBI:137480; EC=4.2.1.17;
CC         Evidence={ECO:0000269|PubMed:11706039};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC         Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489;
CC         EC=5.3.3.8; Evidence={ECO:0000269|PubMed:11706039};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC         Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097;
CC         EC=5.3.3.8; Evidence={ECO:0000269|PubMed:11706039};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA;
CC         Xref=Rhea:RHEA:21760, ChEBI:CHEBI:57315, ChEBI:CHEBI:57316;
CC         EC=5.1.2.3; Evidence={ECO:0000250|UniProtKB:Q39659,
CC         ECO:0000269|PubMed:11706039};
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         Evidence={ECO:0000269|PubMed:11706039};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC   -!- SUBUNIT: Monomer. {ECO:0000303|PubMed:11706039, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}. Cytoplasm, cytoskeleton
CC       {ECO:0000305}.
CC   -!- DOMAIN: The epimerase and isomerase activities are contained in the N-
CC       terminal region while the dehydrogenase activity is in the C-terminal
CC       region. {ECO:0000250|UniProtKB:Q39659}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC       dehydrogenase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL35606.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAQ13901.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF442962; AAL35606.1; ALT_FRAME; mRNA.
DR   EMBL; AP004771; BAD21833.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF08450.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS78079.1; -; Genomic_DNA.
DR   EMBL; AF220609; AAQ13901.1; ALT_INIT; mRNA.
DR   RefSeq; XP_015625624.1; XM_015770138.1.
DR   AlphaFoldDB; Q8W1L6; -.
DR   SMR; Q8W1L6; -.
DR   STRING; 39947.Q8W1L6; -.
DR   PaxDb; 39947-Q8W1L6; -.
DR   EnsemblPlants; Os02t0274100-01; Os02t0274100-01; Os02g0274100.
DR   GeneID; 4328997; -.
DR   Gramene; Os02t0274100-01; Os02t0274100-01; Os02g0274100.
DR   KEGG; osa:4328997; -.
DR   eggNOG; KOG1683; Eukaryota.
DR   HOGENOM; CLU_009834_16_3_1; -.
DR   InParanoid; Q8W1L6; -.
DR   OMA; YNGAAMG; -.
DR   OrthoDB; 622692at2759; -.
DR   PlantReactome; R-OSA-1119445; Beta-alanine biosynthesis II.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   ExpressionAtlas; Q8W1L6; baseline and differential.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0018812; F:3-hydroxyacyl-CoA dehydratase activity; IDA:UniProtKB.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; ISS:UniProtKB.
DR   GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; ISS:UniProtKB.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IDA:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IDA:UniProtKB.
DR   CDD; cd06558; crotonase-like; 1.
DR   Gene3D; 1.10.1040.50; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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-like_C_sf.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23309; 3-HYDROXYACYL-COA DEHYROGENASE; 1.
DR   PANTHER; PTHR23309:SF49; PEROXISOMAL FATTY ACID BETA-OXIDATION MULTIFUNCTIONAL PROTEIN AIM1; 1.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
DR   Genevisible; Q8W1L6; OS.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; Fatty acid metabolism;
KW   Isomerase; Lipid metabolism; Lyase; Microtubule; Multifunctional enzyme;
KW   NAD; Oxidoreductase; Peroxisome; Reference proteome; RNA-binding.
FT   CHAIN           1..726
FT                   /note="Peroxisomal fatty acid beta-oxidation
FT                   multifunctional protein"
FT                   /id="PRO_0000109252"
FT   CONFLICT        178
FT                   /note="G -> R (in Ref. 5; AAQ13901)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        345
FT                   /note="L -> R (in Ref. 1; AAL35606)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        384
FT                   /note="S -> C (in Ref. 1; AAL35606)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   726 AA;  78461 MW;  AFB6E3D2AD02E03E CRC64;
     MAGAIRVTME VGADGVAVVT ICNPPVNALH PIIIQGLKEK YAEAMDRDDV KAIVLTGAGG
     KFCGGFDINV FTEVHKTGNV SLMPDVSVEL VSNLMEAGKK PSVAAIQGLA LGGGLELTMG
     CHARISTPEA QLGLPELTLG IIPGFGGTQR LPRLVGLPKA IEMMLQSKFI TAKEGKEGGL
     VDALCSPDEL IKMSRLWALE IANYRKPWIR SLARTDRLGS LSEARSVLNS ARQQAKKVAA
     NLPQHQACLD VMEEGVLCGG HAGVLKEAKV FKELVLSPTS KALVHAFFAQ RLTTKVPGVT
     DVQLKPRKIR KVAVIGGGLM GSGIATALLV SNTSVVLKEV NPQFLQRGQK MIAANLEGLV
     KRGSLTKDKM NKAMSLLKGA LDYSDFKDVD MVIEAVIEKI PLKQSIFSDL EKVCPPHCIL
     ATNTSTIDLN VVGEKTNSQD RIIGAHFFSP AHIMPLLEIV RTEKTSPQAI LDLITVGKMI
     KKVPVVVGNC TGFAVNRTFF PYTQGSHLLV SIGIDVFRID RVISSFGMPM GPFQLQDLAG
     YGVALAVKDI YAAAFGTRNL DSNLVDLMVQ NGRQGKSNGK GYYLYEKGGK PKPDPSVQVV
     IDEYRRCAKT MPGGKPVTLS DQDILEMIFF PVVNEACRVM DENVVIRASD LDIASILGMG
     FPKFRGGLVF WADTIGAPYI HSKLSKWTEI YGDFFKPSSY LEDRAKRSLP LSAPNATQQA
     SSRSRM
//