MFP_ORYSJ
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 03-AUG-2022, entry version 129.
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; 4530.OS02T0274100-01; -.
DR PaxDb; Q8W1L6; -.
DR PRIDE; 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; TGAGWPF; -.
DR OrthoDB; 219667at2759; -.
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 Genevisible; Q8W1L6; OS.
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 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; IPR033346; AIM1-like.
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:SF36; PTHR23309:SF36; 1.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF48179; SSF48179; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00067; 3HCDH; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
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
