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Q39659 (MFPA_CUCSA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glyoxysomal fatty acid beta-oxidation multifunctional protein MFP-a

Including the following 2 domains:

  1. Enoyl-CoA hydratase/3-2-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase
    EC=4.2.1.17
    EC=5.1.2.3
    EC=5.3.3.8
  2. 3-hydroxyacyl-CoA dehydrogenase
    EC=1.1.1.35
OrganismCucumis sativus (Cucumber)
Taxonomic identifier3659 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeBenincaseaeCucumis

Protein attributes

Sequence length725 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O. Ref.1

(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA. Ref.1

(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA. Ref.1

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH. Ref.1

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subcellular location

Glyoxysome Ref.1.

Domain

The epimerase and isomerase activities are contained in the N-terminal region while the dehydrogenase activity is in the C-terminal region. Ref.1

Sequence similarities

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.

In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 725725Glyoxysomal fatty acid beta-oxidation multifunctional protein MFP-a
PRO_0000109251

Sequences

Sequence LengthMass (Da)Tools
Q39659 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D7C7943A51AFE7DB

FASTA72579,170
        10         20         30         40         50         60 
MGSNAKGRTV MEVGTDGVAI ITIINPPVNS LSFDVLFSLR DSYEQALRRD DVKAIVVTGA 

        70         80         90        100        110        120 
KGKFSGGFDI TAFGVLQGGK GEQPNVRNIS IEMITDIFEA ARKPAVAAID GLALGGGLEV 

       130        140        150        160        170        180 
AMACHARIST PTAQLGLPEL QLGIIPGFGG TQRLPRLVGL SKALEMMLTS KPIKGQEAHS 

       190        200        210        220        230        240 
LGLVDAIVPP EELINTARRW ALEILERRRP WVHSLHRTDK LESLAEARKI FNLARAQAKK 

       250        260        270        280        290        300 
QYPNLKHTIA CIDAVETGVV SGPRAGLWKE AEEFQGLLHS DTCKSLIHIF FAQRSTTKVP 

       310        320        330        340        350        360 
GVTDLGLVPR QIKKVAIVGG GLMGSGIATA LILSNYHVVL KEVNDKFLQA GIDRVRANLQ 

       370        380        390        400        410        420 
SRVKKGNMTN EKFEKSISLL KGVLNYESFK DVDMVIEAVI ENVSLKQQIF SDLEKYCPPH 

       430        440        450        460        470        480 
CMLATNTSTI DLELIGERIK SRDRIIGAHF FSPAHIMPLL EIVRTKHTAA QVIVDLLDVG 

       490        500        510        520        530        540 
KNIKKTPVVV GNCTGFAVNR MFFPYSQAAI LLAEHGVDPY QIDRAISKFG MPMGPFRLCD 

       550        560        570        580        590        600 
LVGFGVAAAT ASQFVQAFPE RTYKSMLIPL MQEDKNAGES TRKGFYVYDK NRKAGPNPEL 

       610        620        630        640        650        660 
KKYIEKARNS SGVSVDPKLT KLPEKDIVEM IFFPVVNEAC RVLAEGIAVK AADLDIAGVM 

       670        680        690        700        710        720 
GMGFPSYRGG LMFWADSLGS NYIYSRLEEW SKQYGGFFKP CGYLAERAVQ GATLSAPGGH 


AKPRM 

« Hide

References

[1]"Domains of the tetrafunctional protein acting in glyoxysomal fatty acid beta oxidation. Demonstration of epimerase and isomerase activities on a peptide lacking hydratase activity."
Preisig-Mueller R., Guehnemann-Schaefer K., Kindl H.
J. Biol. Chem. 269:20475-20481(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
Tissue: Seedling cotyledon.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78996 mRNA. Translation: CAA55630.1.
PIRT10464.
RefSeqXP_004168411.1. XM_004168363.1.

3D structure databases

ProteinModelPortalQ39659.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ39659.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID101210295.
KEGGcsv:101210295.

Phylogenomic databases

KOK10527.

Enzyme and pathway databases

UniPathwayUPA00659.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
InterProIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMFPA_CUCSA
AccessionPrimary (citable) accession number: Q39659
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways