MFPA_CUCSA
ID MFPA_CUCSA Reviewed; 725 AA.
AC Q39659;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
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 Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659 {ECO:0000312|EMBL:CAA55630.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Seedling cotyledon;
RX PubMed=8051146; DOI=10.1016/s0021-9258(17)32017-3;
RA Preisig-Mueller R., Guehnemann-Schaefer K., Kindl H.;
RT "Domains of the tetrafunctional protein acting in glyoxysomal fatty acid
RT beta oxidation. Demonstration of epimerase and isomerase activities on a
RT peptide lacking hydratase activity.";
RL J. Biol. Chem. 269:20475-20481(1994).
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:8051146};
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:8051146};
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:8051146};
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:8051146};
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:0000269|PubMed:8051146};
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:8051146};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- SUBCELLULAR LOCATION: Glyoxysome {ECO:0000269|PubMed:8051146}.
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:0000269|PubMed:8051146}.
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}.
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DR EMBL; X78996; CAA55630.1; -; mRNA.
DR PIR; T10464; T10464.
DR RefSeq; NP_001292693.1; NM_001305764.1.
DR AlphaFoldDB; Q39659; -.
DR SMR; Q39659; -.
DR STRING; 3659.XP_004168410.1; -.
DR PRIDE; Q39659; -.
DR EnsemblPlants; KGN47371; KGN47371; Csa_6G306330.
DR GeneID; 101210295; -.
DR Gramene; KGN47371; KGN47371; Csa_6G306330.
DR KEGG; csv:101210295; -.
DR eggNOG; KOG1683; Eukaryota.
DR UniPathway; UPA00659; -.
DR GO; GO:0009514; C:glyoxysome; NAS:UniProtKB.
DR GO; GO:0018812; F:3-hydroxyacyl-CoA dehydratase activity; IDA:UniProtKB.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IDA:UniProtKB.
DR GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IDA:UniProtKB.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; 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; 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 1: Evidence at protein 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_0000109251"
SQ SEQUENCE 725 AA; 79170 MW; D7C7943A51AFE7DB CRC64;
MGSNAKGRTV MEVGTDGVAI ITIINPPVNS LSFDVLFSLR DSYEQALRRD DVKAIVVTGA
KGKFSGGFDI TAFGVLQGGK GEQPNVRNIS IEMITDIFEA ARKPAVAAID GLALGGGLEV
AMACHARIST PTAQLGLPEL QLGIIPGFGG TQRLPRLVGL SKALEMMLTS KPIKGQEAHS
LGLVDAIVPP EELINTARRW ALEILERRRP WVHSLHRTDK LESLAEARKI FNLARAQAKK
QYPNLKHTIA CIDAVETGVV SGPRAGLWKE AEEFQGLLHS DTCKSLIHIF FAQRSTTKVP
GVTDLGLVPR QIKKVAIVGG GLMGSGIATA LILSNYHVVL KEVNDKFLQA GIDRVRANLQ
SRVKKGNMTN EKFEKSISLL KGVLNYESFK DVDMVIEAVI ENVSLKQQIF SDLEKYCPPH
CMLATNTSTI DLELIGERIK SRDRIIGAHF FSPAHIMPLL EIVRTKHTAA QVIVDLLDVG
KNIKKTPVVV GNCTGFAVNR MFFPYSQAAI LLAEHGVDPY QIDRAISKFG MPMGPFRLCD
LVGFGVAAAT ASQFVQAFPE RTYKSMLIPL MQEDKNAGES TRKGFYVYDK NRKAGPNPEL
KKYIEKARNS SGVSVDPKLT KLPEKDIVEM IFFPVVNEAC RVLAEGIAVK AADLDIAGVM
GMGFPSYRGG LMFWADSLGS NYIYSRLEEW SKQYGGFFKP CGYLAERAVQ GATLSAPGGH
AKPRM
