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Q39659

- MFPA_CUCSA

UniProt

Q39659 - MFPA_CUCSA

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Protein
Glyoxysomal fatty acid beta-oxidation multifunctional protein MFP-a
Gene
N/A
Organism
Cucumis sativus (Cucumber)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.1 Publication
(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.1 Publication
(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.1 Publication
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.1 Publication

Pathwayi

GO - Molecular functioni

  1. 3-hydroxyacyl-CoA dehydratase activity Source: UniProtKB
  2. 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB-EC
  3. 3-hydroxybutyryl-CoA epimerase activity Source: UniProtKB
  4. coenzyme binding Source: InterPro
  5. dodecenoyl-CoA delta-isomerase activity Source: UniProtKB
  6. enoyl-CoA hydratase activity Source: UniProtKB

GO - Biological processi

  1. fatty acid beta-oxidation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyoxysomal fatty acid beta-oxidation multifunctional protein MFP-a
Including the following 2 domains:
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)
3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.35)
OrganismiCucumis sativus (Cucumber)
Taxonomic identifieri3659 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeBenincaseaeCucumis

Subcellular locationi

Glyoxysome 1 Publication

GO - Cellular componenti

  1. glyoxysome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Glyoxysome, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 725725Glyoxysomal fatty acid beta-oxidation multifunctional protein MFP-a
PRO_0000109251Add
BLAST

Proteomic databases

PRIDEiQ39659.

Structurei

3D structure databases

ProteinModelPortaliQ39659.

Family & Domainsi

Domaini

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

Sequence similaritiesi

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.

Phylogenomic databases

KOiK10527.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR006180. 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]
PfamiPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q39659-1 [UniParc]FASTAAdd to Basket

« Hide

MGSNAKGRTV MEVGTDGVAI ITIINPPVNS LSFDVLFSLR DSYEQALRRD    50
DVKAIVVTGA KGKFSGGFDI TAFGVLQGGK GEQPNVRNIS IEMITDIFEA 100
ARKPAVAAID GLALGGGLEV AMACHARIST PTAQLGLPEL QLGIIPGFGG 150
TQRLPRLVGL SKALEMMLTS KPIKGQEAHS LGLVDAIVPP EELINTARRW 200
ALEILERRRP WVHSLHRTDK LESLAEARKI FNLARAQAKK QYPNLKHTIA 250
CIDAVETGVV SGPRAGLWKE AEEFQGLLHS DTCKSLIHIF FAQRSTTKVP 300
GVTDLGLVPR QIKKVAIVGG GLMGSGIATA LILSNYHVVL KEVNDKFLQA 350
GIDRVRANLQ SRVKKGNMTN EKFEKSISLL KGVLNYESFK DVDMVIEAVI 400
ENVSLKQQIF SDLEKYCPPH CMLATNTSTI DLELIGERIK SRDRIIGAHF 450
FSPAHIMPLL EIVRTKHTAA QVIVDLLDVG KNIKKTPVVV GNCTGFAVNR 500
MFFPYSQAAI LLAEHGVDPY QIDRAISKFG MPMGPFRLCD LVGFGVAAAT 550
ASQFVQAFPE RTYKSMLIPL MQEDKNAGES TRKGFYVYDK NRKAGPNPEL 600
KKYIEKARNS SGVSVDPKLT KLPEKDIVEM IFFPVVNEAC RVLAEGIAVK 650
AADLDIAGVM GMGFPSYRGG LMFWADSLGS NYIYSRLEEW SKQYGGFFKP 700
CGYLAERAVQ GATLSAPGGH AKPRM 725
Length:725
Mass (Da):79,170
Last modified:November 1, 1996 - v1
Checksum:iD7C7943A51AFE7DB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X78996 mRNA. Translation: CAA55630.1.
PIRiT10464.
RefSeqiXP_004168411.1. XM_004168363.1.

Genome annotation databases

GeneIDi101210295.
KEGGicsv:101210295.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X78996 mRNA. Translation: CAA55630.1 .
PIRi T10464.
RefSeqi XP_004168411.1. XM_004168363.1.

3D structure databases

ProteinModelPortali Q39659.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q39659.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 101210295.
KEGGi csv:101210295.

Phylogenomic databases

KOi K10527.

Enzyme and pathway databases

UniPathwayi UPA00659 .

Family and domain databases

Gene3Di 1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
InterProi IPR006180. 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 ]
Pfami PF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view ]
SUPFAMi SSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
PROSITEi PS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiMFPA_CUCSA
AccessioniPrimary (citable) accession number: Q39659
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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