MFPA_BRANA
ID MFPA_BRANA Reviewed; 725 AA.
AC O49809;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Glyoxysomal fatty acid beta-oxidation multifunctional protein MFP-a;
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;
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000312|EMBL:CAA04386.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Global;
RA Geshi N., Rechinger K.B., Brandt A.;
RT "A full-length cDNA clone from Brassica napus encoding a multifunctional
RT enzyme of the glyoxysomal fatty acid beta-oxidation.";
RL (er) Plant Gene Register PGR98-067(1998).
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:0000250|UniProtKB:Q39659};
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:0000250|UniProtKB:Q39659};
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;
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;
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 -!- 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:0000250|UniProtKB:Q39659};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- SUBCELLULAR LOCATION: Glyoxysome {ECO:0000250}.
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}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ000886; CAA04386.1; -; mRNA.
DR PIR; T08017; T08017.
DR RefSeq; NP_001302620.1; NM_001315691.1.
DR AlphaFoldDB; O49809; -.
DR SMR; O49809; -.
DR PRIDE; O49809; -.
DR GeneID; 106389027; -.
DR KEGG; bna:106389027; -.
DR UniPathway; UPA00659; -.
DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0018812; F:3-hydroxyacyl-CoA dehydratase activity; ISS:UniProtKB.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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; ISS:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS: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; 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 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 2: Evidence at transcript level;
KW Fatty acid metabolism; Glyoxysome; Isomerase; Lipid metabolism; Lyase;
KW Multifunctional enzyme; NAD; Oxidoreductase; Peroxisome.
FT CHAIN 1..725
FT /note="Glyoxysomal fatty acid beta-oxidation
FT multifunctional protein MFP-a"
FT /id="PRO_0000109250"
FT MOTIF 723..725
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT ACT_SITE 139
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
SQ SEQUENCE 725 AA; 79023 MW; 6627C52D433EA976 CRC64;
MASRTKGTTT IEVGADGVAV ITLINPPVNS LSFDVLYSLK SNYEEALSRN DVKAIVVTGA
KGKFSGGFDI SGFGEIQKGT MKEPKVGYIS IDILTDLLEA AKKPSVAAID GLALGGGLEL
SMACHARISA PGAQLGLPEL QLGVIPGFGG TQRLPRLVGL TKALEMILTS KPVKAEEGHS
LGLIDAVVPP AELLNAARRW ALDIAERRKP WVSSVLKTDK LPPLGEAREI LKFAKDQTRR
QAPNMKHPLM CLEAVEVGIV SGSRAGLEKE AQVGSEVINL DTTKGLIHVF FSQRGTTKVP
GVTDRGLVPR KINKVAIIGG GLMGSGIATA LILSNYSVIL KEVNEKFLEA GIGRVKANLQ
SRVKKGKMSK EKFEKTMSLL KGSLDYESFR DVDMVIEAVI ENISLKQQIF ADLEKYCPQH
CILASNTSTI DLNKIGERTK SQDRIIGAHF FSPAHVMPLL EIVRTNHTSA QVIVDLLDVG
KKIRKTPVVV GNCTGFAVNR MFFPYTQAAM FLVEHGTDPY LIDKAVSKFG MPMGPFRLCD
LVGFGVAIAT ATQFIENFPE RTYKSMIIPL MQEDKRAGEA TRKGFYLYDD RRKAKPDPEI
KNYIDKARSV SGAKPDPKLE KLSEKEIIEM TFFPVVNEAC RVFAEGIAVK AADLDIAGIF
GMGFPPYRGG IMFWADSIGS KYIYSKLEEW SKAYGEFFKP CAFLAERGSK GAPLSAPLEQ
SRSRL
